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1kno

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[[Image:1kno.gif|left|200px]]
[[Image:1kno.gif|left|200px]]
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{{Structure
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|LIGAND= <scene name='pdbligand=PNP:METHYL-PHOSPHONIC+ACID+MONO-(4-NITRO-PHENYL)+ESTER'>PNP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kno FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kno OCA], [http://www.ebi.ac.uk/pdbsum/1kno PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kno RCSB]</span>
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'''CRYSTAL STRUCTURE OF THE COMPLEX OF A CATALYTIC ANTIBODY FAB WITH A TRANSITION STATE ANALOG: STRUCTURAL SIMILARITIES IN ESTERASE-LIKE ABZYMES'''
'''CRYSTAL STRUCTURE OF THE COMPLEX OF A CATALYTIC ANTIBODY FAB WITH A TRANSITION STATE ANALOG: STRUCTURAL SIMILARITIES IN ESTERASE-LIKE ABZYMES'''
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[[Category: Gigant, B.]]
[[Category: Gigant, B.]]
[[Category: Knossow, M.]]
[[Category: Knossow, M.]]
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[[Category: catalytic antibody]]
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[[Category: Catalytic antibody]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:57:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:51:01 2008''
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Revision as of 19:57, 2 May 2008

Template:STRUCTURE 1kno

CRYSTAL STRUCTURE OF THE COMPLEX OF A CATALYTIC ANTIBODY FAB WITH A TRANSITION STATE ANALOG: STRUCTURAL SIMILARITIES IN ESTERASE-LIKE ABZYMES


Overview

The x-ray structure of the complex of a catalytic antibody Fab fragment with a phosphonate transition-state analog has been determined. The antibody (CNJ206) catalyzes the hydrolysis of p-nitrophenyl esters with significant rate enhancement and substrate specificity. Comparison of this structure with that of the uncomplexed Fab fragment suggests hapten-induced conformational changes: the shape of the combining site changes from a shallow groove in the uncomplexed Fab to a deep pocket where the hapten is buried. Three hydrogen-bond donors appear to stabilize the charged phosphonate group of the hapten: two NH groups of the heavy (H) chain complementarity-determining region 3 (H3 CDR) polypeptide chain and the side-chain of histidine-H35 in the H chain (His-H35) in the H1 CDR. The combining site shows striking structural similarities to that of antibody 17E8, which also has esterase activity. Both catalytic antibody ("abzyme") structures suggest that oxyanion stabilization plays a significant role in their rate acceleration. Additional catalytic groups that improve efficiency are not necessarily induced by the eliciting hapten; these groups may occur because of the variability in the combining sites of different monoclonal antibodies that bind to the same hapten.

About this Structure

1KNO is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the complex of a catalytic antibody Fab fragment with a transition state analog: structural similarities in esterase-like catalytic antibodies., Charbonnier JB, Carpenter E, Gigant B, Golinelli-Pimpaneau B, Eshhar Z, Green BS, Knossow M, Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11721-5. PMID:8524836 Page seeded by OCA on Fri May 2 22:57:19 2008

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