1yed

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(New page: 200px<br /> <applet load="1yed" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yed, resolution 3.1&Aring;" /> '''STRUCTURE OF A CATAL...)
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<applet load="1yed" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1yed, resolution 3.1&Aring;" />
caption="1yed, resolution 3.1&Aring;" />
'''STRUCTURE OF A CATALYTIC ANTIBODY IGG2A FAB FRAGMENT (D2.4)'''<br />
'''STRUCTURE OF A CATALYTIC ANTIBODY IGG2A FAB FRAGMENT (D2.4)'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1YED is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with PNB as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YED OCA].
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1YED is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=PNB:'>PNB</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YED OCA].
==Reference==
==Reference==
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[[Category: transition state analogue]]
[[Category: transition state analogue]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:45:12 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:29 2008''

Revision as of 14:04, 21 February 2008


1yed, resolution 3.1Å

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STRUCTURE OF A CATALYTIC ANTIBODY IGG2A FAB FRAGMENT (D2.4)

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

1YED is a Protein complex structure of sequences from Mus musculus with 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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