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| - | [[Image:1eap.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1eap| PDB=1eap | SCENE= }} | | {{STRUCTURE_1eap| PDB=1eap | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF A CATALYTIC ANTIBODY WITH A SERINE PROTEASE ACTIVE SITE'''
| + | ===CRYSTAL STRUCTURE OF A CATALYTIC ANTIBODY WITH A SERINE PROTEASE ACTIVE SITE=== |
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| - | ==Overview==
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| - | The three-dimensional structure of an unusually active hydrolytic antibody with a phosphonate transition state analog (hapten) bound to the active site has been solved to 2.5 A resolution. The antibody (17E8) catalyzes the hydrolysis of norleucine and methionine phenyl esters and is selective for amino acid esters that have the natural alpha-carbon L configuration. A plot of the pH-dependence of the antibody-catalyzed reaction is bell-shaped with an activity maximum at pH 9.5; experiments on mechanism lend support to the formation of a covalent acyl-antibody intermediate. The structural and kinetic data are complementary and support a hydrolytic mechanism for the antibody that is remarkably similar to that of the serine proteases. The antibody active site contains a Ser-His dyad structure proximal to the phosphorous atom of the bound hapten that resembles two of the three components of the Ser-His-Asp catalytic triad of serine proteases. The antibody active site also contains a Lys residue to stabilize oxyanion formation, and a hydrophobic binding pocket for specific substrate recognition of norleucine and methionine side chains. The structure identifies active site residues that mediate catalysis and suggests specific mutations that may improve the catalytic efficiency of the antibody. This high resolution structure of a catalytic antibody-hapten complex shows that antibodies can converge on active site structures that have arisen through natural enzyme evolution. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8066444}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8066444 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8066444}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Zhou, G W.]] | | [[Category: Zhou, G W.]] |
| | [[Category: Catalytic antibody]] | | [[Category: Catalytic antibody]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:52:38 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:25:08 2008'' |
Revision as of 21:25, 30 June 2008
Template:STRUCTURE 1eap
CRYSTAL STRUCTURE OF A CATALYTIC ANTIBODY WITH A SERINE PROTEASE ACTIVE SITE
Template:ABSTRACT PUBMED 8066444
About this Structure
1EAP is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a catalytic antibody with a serine protease active site., Zhou GW, Guo J, Huang W, Fletterick RJ, Scanlan TS, Science. 1994 Aug 19;265(5175):1059-64. PMID:8066444
Page seeded by OCA on Tue Jul 1 00:25:08 2008
