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2bjm

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[[Category: promiscuity]]
[[Category: promiscuity]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:12:10 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:40:07 2007''

Revision as of 14:35, 30 October 2007


2bjm, resolution 2.150Å

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SPE7:ANTHRONE COMPLEX

Overview

Induced fit is a predominant phenomenon in protein-ligand interactions, yet it is invariably attributed without establishing the existence, let, alone the structure, of the initial, low-affinity encounter complex. We, determined the crystal structure of the encounter complex on the pathway, of ligand binding by IgE antibody SPE7. We show that this complex is, formed by a wide range of ligands that initially bind with identical, affinity. Nonspecific ligands rapidly dissociate, whereupon the antibody, isomerizes to a nonbinding isomer. Specific ligand complexes, however, slowly isomerize to give a high-affinity complex. This isomerization, involves backbone and side-chain rearrangements of up to 14 A and the, formation of specific hydrogen bonds. The postbinding conformational, switch, ... [(full description)]

About this Structure

2BJM is a [Single protein] structure of sequence from [Rattus rattus] with ANF as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structure and kinetics of a transient antibody binding intermediate reveal a kinetic discrimination mechanism in antigen recognition., James LC, Tawfik DS, Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12730-5. Epub 2005 Aug 29. PMID:16129832

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