1yee | pdb_00001yee

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Revision as of 07:38, 18 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1yee" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yee, resolution 2.2Å" /> '''STRUCTURE OF A CATAL...)
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File:1yee.gif


1yee, resolution 2.2Å

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STRUCTURE OF A CATALYTIC ANTIBODY, IGG2A FAB FRAGMENT (D2.5)

Overview

The x-ray structures of three esterase-like catalytic antibodies, identified by screening for catalytic activity the entire hybridoma, repertoire, elicited in response to a phosphonate transition state analog, (TSA) hapten, were analyzed. The high resolution structures account for, catalysis by transition state stabilization, and in all three antibodies a, tyrosine residue participates in the oxyanion hole. Despite significant, conformational differences in their combining sites, the three antibodies, which are the most efficient among those elicited, achieve catalysis in, essentially the same mode, suggesting that evolution for binding to a, single TSA followed by screening for catalysis lead to antibodies with, structural convergence.

About this Structure

1YEE is a Protein complex structure of sequences from Mus musculus with PNB as ligand. Full crystallographic information is available from OCA.

Reference

Structural convergence in the active sites of a family of catalytic antibodies., Charbonnier JB, Golinelli-Pimpaneau B, Gigant B, Tawfik DS, Chap R, Schindler DG, Kim SH, Green BS, Eshhar Z, Knossow M, Science. 1997 Feb 21;275(5303):1140-2. PMID:9027317

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