<templatestyles src="Module:Hatnote/styles.css"></templatestyles>
<templatestyles src="Module:Infobox/styles.css"></templatestyles>
Lysozyme |
PDB rendering based on 132l.
|
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
133L, 134L, 1B5U, 1B5V, 1B5W, 1B5X, 1B5Y, 1B5Z, 1B7L, 1B7M, 1B7N, 1B7O, 1B7P, 1B7Q, 1B7R, 1B7S, 1BB3, 1BB4, 1BB5, 1C43, 1C45, 1C46, 1C7P, 1CJ6, 1CJ7, 1CJ8, 1CJ9, 1CKC, 1CKD, 1CKF, 1CKG, 1CKH, 1D6P, 1D6Q, 1DI3, 1DI4, 1DI5, 1EQ4, 1EQ5, 1EQE, 1GAY, 1GAZ, 1GB0, 1GB2, 1GB3, 1GB5, 1GB6, 1GB7, 1GB8, 1GB9, 1GBO, 1GBW, 1GBX, 1GBY, 1GBZ, 1GDW, 1GDX, 1GE0, 1GE1, 1GE2, 1GE3, 1GE4, 1GEV, 1GEZ, 1GF0, 1GF3, 1GF4, 1GF5, 1GF6, 1GF7, 1GF8, 1GF9, 1GFA, 1GFE, 1GFG, 1GFH, 1GFJ, 1GFK, 1GFR, 1GFT, 1GFU, 1GFV, 1HNL, 1I1Z, 1I20, 1I22, 1INU, 1IOC, 1IP1, 1IP2, 1IP3, 1IP4, 1IP5, 1IP6, 1IP7, 1IWT, 1IWU, 1IWV, 1IWW, 1IWX, 1IWY, 1IWZ, 1IX0, 1IY3, 1IY4, 1JKA, 1JKB, 1JKC, 1JKD, 1JSF, 1JWR, 1LAA, 1LHH, 1LHI, 1LHJ, 1LHK, 1LHL, 1LHM, 1LMT, 1LOZ, 1LYY, 1LZ1, 1LZ4, 1LZ5, 1LZ6, 1LZR, 1LZS, 1OP9, 1OUA, 1OUB, 1OUC, 1OUD, 1OUE, 1OUF, 1OUG, 1OUH, 1OUI, 1OUJ, 1QSW, 1RE2, 1REM, 1REX, 1REY, 1REZ, 1TAY, 1TBY, 1TCY, 1TDY, 1UBZ, 1W08, 1WQM, 1WQN, 1WQO, 1WQP, 1WQQ, 1WQR, 1YAM, 1YAN, 1YAO, 1YAP, 1YAQ, 207L, 208L, 2BQA, 2BQB, 2BQC, 2BQD, 2BQE, 2BQF, 2BQG, 2BQH, 2BQI, 2BQJ, 2BQK, 2BQL, 2BQM, 2BQN, 2BQO, 2HEA, 2HEB, 2HEC, 2HED, 2HEE, 2HEF, 2LHM, 2MEA, 2MEB, 2MEC, 2MED, 2MEE, 2MEF, 2MEG, 2MEH, 2MEI, 2NWD, 2ZIJ, 2ZIK, 2ZIL, 2ZWB, 3EBA, 3FE0, 3LHM, 3LN2, 4I0C, 4ML7, 4R0P
|
|
|
Symbols |
LYZ ; LZM |
External IDs |
OMIM: 153450 MGI: 96897 HomoloGene: 121490 GeneCards: LYZ Gene |
EC number |
3.2.1.17 |
|
|
More reference expression data |
Species |
Human |
Mouse |
Entrez |
4069 |
17105 |
Ensembl |
ENSG00000090382 |
ENSMUSG00000069516 |
UniProt |
P61626 |
P08905 |
RefSeq (mRNA) |
NM_000239 |
NM_017372 |
RefSeq (protein) |
NP_000230 |
NP_059068 |
Location (UCSC) |
Chr 12:
69.35 – 69.35 Mb |
Chr 10:
117.28 – 117.28 Mb |
PubMed search |
[1] |
[2] |
|
Lysozymes, also known as muramidase or N-acetylmuramide glycanhydrolase, are glycoside hydrolases. These are enzymes (EC 3.2.1.17) that damage bacterial cell walls by catalyzing hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. Lysozyme is abundant in a number of secretions, such as tears, saliva, human milk, and mucus. It is also present in cytoplasmic granules of the macrophages and the polymorphonuclear neutrophils (PMNs). Large amounts of lysozyme can be found in egg white. C-type lysozymes are closely related to alpha-lactalbumin in sequence and structure, making them part of the same family. In humans, the lysozyme enzyme is encoded by the LYZ gene.[1][2]
Function
The enzyme functions by attacking peptidoglycans (found in the cell walls of bacteria, especially Gram-positive bacteria) and hydrolyzing the glycosidic bond that connects N-acetylmuramic acid with the fourth carbon atom of N-acetylglucosamine. It does this by binding to the peptidoglycan molecule in the binding site within the prominent cleft between its two domains. This causes the substrate molecule to adopt a strained conformation similar to that of the transition state.[3] According to Phillips-Mechanism, the lysozyme binds to a hexasaccharide. The lysozyme then distorts the fourth sugar in hexasaccharide (the D ring) into a half-chair conformation. In this stressed state, the glycosidic bond is easily broken.
The amino acid side-chains glutamic acid 35 (Glu35) and aspartate 52 (Asp52) have been found to be critical to the activity of this enzyme. Glu35 acts as a proton donor to the glycosidic bond, cleaving the C-O bond in the substrate, whereas Asp52 acts as a nucleophile to generate a glycosyl enzyme intermediate. The glycosyl enzyme intermediate then reacts with a water molecule, to give the product of hydrolysis and leaving the enzyme unchanged.[4]
Mechanism of lysozyme action
<templatestyles src="Module:Hatnote/styles.css"></templatestyles>
Role in disease
Lysozyme is part of the innate immune system. Reduced lysozyme levels have been associated with bronchopulmonary dysplasia in newborns.[5] Children fed infant formula lacking lysozyme in their diet have three times the rate of diarrheal disease.[6][not in citation given] Since lysozyme is a natural form of protection from Gram-positive pathogens like Bacillus and Streptococcus,[7] a deficiency due to infant formula feeding can lead to increased incidence of disease[citation needed]. Whereas the skin is a protective barrier due to its dryness and acidity, the conjunctiva (membrane covering the eye) is, instead, protected by secreted enzymes, mainly lysozyme and defensin. However, when these protective barriers fail, conjunctivitis results.
In certain cancers (especially myelomonocytic leukemia) excessive production of lysozyme by cancer cells can lead to toxic levels of lysozyme in the blood. High lysozyme blood levels can lead to kidney failure and low blood potassium, conditions that may improve or resolve with treatment of the primary malignancy.
Serum lysozyme is much less specific for diagnosis of sarcoidosis than serum Angiotensin Converting Enzyme, since it is more sensitive, it is used as a marker of sarcoidosis disease activity and suitable for disease monitoring in proven cases [8]
History
The antibacterial property of hen egg white, due to the lysozyme it contains, was first observed by Laschtschenko in 1909,[9] although it was not until 1922 that the name 'lysozyme' was coined, by Alexander Fleming (1881–1955), the discoverer of penicillin.[10] Fleming first observed the antibacterial action of lysozyme when he treated bacterial cultures with nasal mucus from a patient suffering from a head cold.[10]
The three-dimensional structure of hen egg white lysozyme was described by David Chilton Phillips (1924–1999) in 1965, when he obtained the first 2-ångström (200 pm) resolution model via X-ray crystallography.[11][12] The structure was publicly presented at a Royal Institution lecture in 1965.[13] Lysozyme was the second protein structure and the first enzyme structure to be solved via X-ray diffraction methods, and the first enzyme to be fully sequenced that contains all twenty common amino acids.[14] As a result of Phillips' elucidation of the structure of lysozyme, it was also the first enzyme to have a detailed, specific mechanism suggested for its method of catalytic action.[15][16][17] This work led Phillips to provide an explanation for how enzymes speed up a chemical reaction in terms of its physical structures. The original mechanism proposed by Phillips was more recently revised.[18]
Chemical synthesis
The first chemical synthesis of a lysozyme protein was attempted by Prof. George W. Kenner and his group at the University of Liverpool in England.[19] This was finally achieved in 2007 by Steve Kent at the University of Chicago who made synthetic functional lysozyme molecule.[20]
See also
References
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Microbiology: A human perspective. Nester, Anderson, Roberts, Nester. 5th Ed. 2007
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ 10.0 10.1 Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
External links
PDB gallery
|
|
133l: ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS
|
|
134l: ROLE OF ARG 115 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME. X-RAY STRUCTURE OF HIS 115 AND GLU 115 MUTANTS
|
|
1b5u: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANT
|
|
1b5v: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS
|
|
1b5w: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS
|
|
1b5x: Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and x-ray analysis of six ser->ala mutants
|
|
1b5y: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS
|
|
1b5z: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS
|
|
1b7l: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
|
|
1b7m: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
|
|
1b7n: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
|
|
1b7o: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
|
|
1b7p: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
|
|
1b7q: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
|
|
1b7r: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
|
|
1b7s: VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES
|
|
1bb3: HUMAN LYSOZYME MUTANT A96L
|
|
1bb4: HUMAN LYSOZYME DOUBLE MUTANT A96L, W109H
|
|
1bb5: HUMAN LYSOZYME MUTANT A96L COMPLEXED WITH CHITOTRIOSE
|
|
1c43: MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES
|
|
1c45: MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES
|
|
1c46: MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES
|
|
1c7p: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME WITH FOUR EXTRA RESIDUES (EAEA) AT THE N-TERMINAL
|
|
1cj6: T11A MUTANT HUMAN LYSOZYME
|
|
1cj7: T11V MUTANT HUMAN LYSOZYME
|
|
1cj8: T40A MUTANT HUMAN LYSOZYME
|
|
1cj9: T40V MUTANT HUMAN LYSOZYME
|
|
1ckc: T43A MUTANT HUMAN LYSOZYME
|
|
1ckd: T43V MUTANT HUMAN LYSOZYME
|
|
1ckf: T52A MUTANT HUMAN LYSOZYME
|
|
1ckg: T52V MUTANT HUMAN LYSOZYME
|
|
1ckh: T70V MUTANT HUMAN LYSOZYME
|
|
1d6p: HUMAN LYSOZYME L63 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL N,N'-DIACETYLCHITOBIOSE
|
|
1d6q: HUMAN LYSOZYME E102 MUTANT LABELLED WITH 2',3'-EPOXYPROPYL GLYCOSIDE OF N-ACETYLLACTOSAMINE
|
|
1di3: ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME
|
|
1di4: ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME
|
|
1di5: ROLE OF AMINO ACID RESIDUES AT TURNS IN THE CONFORMATIONAL STABILITY AND FOLDING OF HUMAN LYSOZYME
|
|
1eq4: CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME
|
|
1eq5: CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME
|
|
1eqe: CRYSTAL STRUCTURES OF SALT BRIDGE MUTANTS OF HUMAN LYSOZYME
|
|
1gay: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gaz: Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions
|
|
1gb0: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gb2: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gb3: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gb5: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gb6: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gb7: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gb8: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gb9: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gbo: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gbw: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gbx: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gby: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gbz: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gdw: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
|
|
1gdx: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
|
|
1ge0: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
|
|
1ge1: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
|
|
1ge2: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
|
|
1ge3: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
|
|
1ge4: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
|
|
1gev: BURIED POLAR MUTANT HUMAN LYSOZYME
|
|
1gez: BURIED POLAR MUTANT HUMAN LYSOZYME
|
|
1gf0: BURIED POLAR MUTANT HUMAN LYSOZYME
|
|
1gf3: BURIED POLAR MUTANT HUMAN LYSOZYME
|
|
1gf4: BURIED POLAR MUTANT HUMAN LYSOZYME
|
|
1gf5: BURIED POLAR MUTANT HUMAN LYSOZYME
|
|
1gf6: BURIED POLAR MUTANT HUMAN LYSOZYME
|
|
1gf7: BURIED POLAR MUTANT HUMAN LYSOZYME
|
|
1gf8: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gf9: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gfa: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gfe: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gfg: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gfh: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gfj: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gfk: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gfr: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gft: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gfu: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1gfv: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1hnl: CRYSTAL STRUCTURE OF A GLUTATHIONYLATED HUMAN LYSOZYME: A FOLDING INTERMEDIATE MIMIC IN THE FORMATION OF A DISULFIDE BOND
|
|
1i1z: MUTANT HUMAN LYSOZYME (Q86D)
|
|
1i20: MUTANT HUMAN LYSOZYME (A92D)
|
|
1i22: MUTANT HUMAN LYSOZYME (A83K/Q86D/A92D)
|
|
1inu: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
|
|
1ioc: CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T
|
|
1ip1: G37A HUMAN LYSOZYME
|
|
1ip2: G48A HUMAN LYSOZYME
|
|
1ip3: G68A HUMAN LYSOZYME
|
|
1ip4: G72A HUMAN LYSOZYME
|
|
1ip5: G105A HUMAN LYSOZYME
|
|
1ip6: G127A HUMAN LYSOZYME
|
|
1ip7: G129A HUMAN LYSOZYME
|
|
1iwt: Crystal Structure Analysis of Human lysozyme at 113K.
|
|
1iwu: Crystal Structure Analysis of Human lysozyme at 127K.
|
|
1iwv: Crystal Structure Analysis of Human lysozyme at 147K.
|
|
1iww: Crystal Structure Analysis of Human lysozyme at 152K.
|
|
1iwx: Crystal Structure Analysis of Human lysozyme at 161K.
|
|
1iwy: Crystal Structure Analysis of Human lysozyme at 170K.
|
|
1iwz: Crystal Structure Analysis of Human lysozyme at 178K.
|
|
1ix0: I59A-3SS human lysozyme
|
|
1iy3: Solution Structure of the Human lysozyme at 4 degree C
|
|
1iy4: Solution structure of the human lysozyme at 35 degree C
|
|
1jka: HUMAN LYSOZYME MUTANT WITH GLU 35 REPLACED BY ASP
|
|
1jkb: HUMAN LYSOZYME MUTANT WITH GLU 35 REPLACED BY ALA
|
|
1jkc: HUMAN LYSOZYME MUTANT WITH TRP 109 REPLACED BY PHE
|
|
1jkd: HUMAN LYSOZYME MUTANT WITH TRP 109 REPLACED BY ALA
|
|
1jsf: FULL-MATRIX LEAST-SQUARES REFINEMENT OF HUMAN LYSOZYME
|
|
1jwr: Crystal structure of human lysozyme at 100 K
|
|
1laa: X-RAY STRUCTURE OF GLU 53 HUMAN LYSOZYME
|
|
1lhh: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
|
|
1lhi: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
|
|
1lhj: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
|
|
1lhk: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
|
|
1lhl: ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
|
|
1lhm: THE CRYSTAL STRUCTURE OF A MUTANT LYSOZYME C77(SLASH)95A WITH INCREASED SECRETION EFFICIENCY IN YEAST
|
|
1lmt: STRUCTURE OF A CONFORMATIONALLY CONSTRAINED ARG-GLY-ASP SEQUENCE INSERTED INTO HUMAN LYSOZYME
|
|
1loz: AMYLOIDOGENIC VARIANT (I56T) VARIANT OF HUMAN LYSOZYME
|
|
1lyy: AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME
|
|
1lz1: REFINEMENT OF HUMAN LYSOZYME AT 1.5 ANGSTROMS RESOLUTION. ANALYSIS OF NON-BONDED AND HYDROGEN-BOND INTERACTIONS
|
|
1lz4: ENTHALPIC DESTABILIZATION OF A MUTANT HUMAN LYSOZYME LACKING A DISULFIDE BRIDGE BETWEEN CYSTEINE-77 AND CYSTEINE-95
|
|
1lz5: STRUCTURAL AND FUNCTIONAL ANALYSES OF THE ARG-GLY-ASP SEQUENCE INTRODUCED INTO HUMAN LYSOZYME
|
|
1lz6: STRUCTURAL AND FUNCTIONAL ANALYSES OF THE ARG-GLY-ASP SEQUENCE INTRODUCED INTO HUMAN LYSOZYME
|
|
1lzr: STRUCTURAL CHANGES OF THE ACTIVE SITE CLEFT AND DIFFERENT SACCHARIDE BINDING MODES IN HUMAN LYSOZYME CO-CRYSTALLIZED WITH HEXA-N-ACETYL-CHITOHEXAOSE AT PH 4.0
|
|
1lzs: STRUCTURAL CHANGES OF THE ACTIVE SITE CLEFT AND DIFFERENT SACCHARIDE BINDING MODES IN HUMAN LYSOZYME CO-CRYSTALLIZED WITH HEXA-N-ACETYL-CHITOHEXAOSE AT PH 4.0
|
|
1op9: Complex of human lysozyme with camelid VHH HL6 antibody fragment
|
|
1oua: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE I56T MUTANT
|
|
1oub: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V100A MUTANT
|
|
1ouc: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT
|
|
1oud: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V121A MUTANT
|
|
1oue: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V125A MUTANT
|
|
1ouf: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V130A MUTANT
|
|
1oug: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V2A MUTANT
|
|
1ouh: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V74A MUTANT
|
|
1oui: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V93A MUTANT
|
|
1ouj: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V99A MUTANT
|
|
1qsw: CRYSTAL STRUCTURE ANALYSIS OF A HUMAN LYSOZYME MUTANT W64C C65A
|
|
1re2: HUMAN LYSOZYME LABELLED WITH TWO 2',3'-EPOXYPROPYL BETA-GLYCOSIDE OF N-ACETYLLACTOSAMINE
|
|
1rem: HUMAN LYSOZYME WITH MAN-B1,4-GLCNAC COVALENTLY ATTACHED TO ASP53
|
|
1rex: NATIVE HUMAN LYSOZYME
|
|
1rey: HUMAN LYSOZYME-N,N'-DIACETYLCHITOBIOSE COMPLEX
|
|
1rez: HUMAN LYSOZYME-N-ACETYLLACTOSAMINE COMPLEX
|
|
1tay: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME
|
|
1tby: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME
|
|
1tcy: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME
|
|
1tdy: DISSECTION OF THE FUNCTIONAL ROLE OF STRUCTURAL ELEMENTS OF TYROSINE-63 IN THE CATALYTIC ACTION OF HUMAN LYSOZYME
|
|
1ubz: Crystal structure of Glu102-mutant human lysozyme doubly labeled with 2',3'-epoxypropyl beta-glycoside of N-acetyllactosamine
|
|
1w08: STRUCTURE OF T70N HUMAN LYSOZYME
|
|
1wqm: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
1wqn: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
1wqo: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
1wqp: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
1wqq: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
1wqr: CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
1yam: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS
|
|
1yan: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS
|
|
1yao: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS
|
|
1yap: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS
|
|
1yaq: CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS
|
|
207l: MUTANT HUMAN LYSOZYME C77A
|
|
208l: MUTANT HUMAN LYSOZYME C77A
|
|
2bqa: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2bqb: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2bqc: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2bqd: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2bqe: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2bqf: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2bqg: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2bqh: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2bqi: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2bqj: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2bqk: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2bql: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2bqm: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2bqn: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2bqo: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2hea: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY
|
|
2heb: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY
|
|
2hec: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY
|
|
2hed: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY
|
|
2hee: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY
|
|
2hef: CONTRIBUTION OF WATER MOLECULES IN THE INTERIOR OF A PROTEIN TO THE CONFORMATIONAL STABILITY
|
|
2lhm: CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE
|
|
2mea: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS
|
|
2meb: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS
|
|
2mec: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS
|
|
2med: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2mee: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2mef: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2meg: CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS.
|
|
2meh: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2mei: CONTRIBUTION OF HYDROPHOBIC EFFECT TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
|
|
2nwd: Structure of chemically synthesized human lysozyme at 1 Angstrom resolution
|
|
3lhm: CRYSTAL STRUCTURES OF THE APO-AND HOLOMUTANT HUMAN LYSOZYMES WITH AN INTRODUCED CA2+ BINDING SITE
|
|
|