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| - | [[Image:1i22.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1i22.png|left|200px]] |
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| | {{STRUCTURE_1i22| PDB=1i22 | SCENE= }} | | {{STRUCTURE_1i22| PDB=1i22 | SCENE= }} |
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| - | '''MUTANT HUMAN LYSOZYME (A83K/Q86D/A92D)'''
| + | ===MUTANT HUMAN LYSOZYME (A83K/Q86D/A92D)=== |
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| - | ==Overview==
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| - | Structural determinants of Ca2+ binding sites within proteins typically comprise several acidic residues in appropriate juxtaposition. Three residues (Ala-83, Gln-86, and Ala-92) in human lysozyme are characteristically mutated to Lys, Asp, and Asp, respectively, in natural Ca2+ binding lysozymes and alpha-lactalbumins. The effects of these mutations on the stability and Ca2+ binding properties of human lysozyme were investigated using calorimetry and were interpreted with crystal structures. The double mutant, in which Glu-86 and Ala-92 were replaced with Asp, clearly showed Ca2+ binding affinity, whereas neither point mutant showed Ca2+ affinity, indicating that both residues are essential. The further mutation of Ala-83 --> Lys did not affect the Ca2+ binding of the double mutant. The point mutations Ala-83 --> Lys and Glu-86 --> Asp did not affect the stability, whereas the mutation Ala-92 --> Asp was about 1.3 kcal/mol less stable. Structural analyses showed that both Asp-86 and Lys-83 were exposed to solvent. Side chains of Asp-86 and Asp-91 were rotated in opposite directions about chi1 angle, as if to reduce the electrostatic repulsion. The charged amino acids at the Ca2+ binding site did not significantly affect stability of the protein, possibly because of the local conformational change of the side chains.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9852096}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9852096 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9852096}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| | [[Category: Mutant human lysozyme]] | | [[Category: Mutant human lysozyme]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:28:53 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:17:49 2008'' |
Revision as of 07:17, 1 July 2008
Template:STRUCTURE 1i22
MUTANT HUMAN LYSOZYME (A83K/Q86D/A92D)
Template:ABSTRACT PUBMED 9852096
About this Structure
1I22 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural and thermodynamic responses of mutations at a Ca2+ binding site engineered into human lysozyme., Kuroki R, Yutani K, J Biol Chem. 1998 Dec 18;273(51):34310-5. PMID:9852096
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