2bj4

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(New page: 200px<br /> <applet load="2bj4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bj4, resolution 2.00&Aring;" /> '''ESTROGEN RECEPTOR A...)
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Revision as of 18:12, 29 October 2007


2bj4, resolution 2.00Å

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ESTROGEN RECEPTOR ALPHA LBD IN COMPLEX WITH A PHAGE-DISPLAY DERIVED PEPTIDE ANTAGONIST

Overview

Recent studies have identified a series of estrogen receptor, (ER)-interacting peptides that recognize sites that are distinct from the, classic coregulator recruitment (AF2) region. Here, we report the, structural and functional characterization of an ERalpha-specific peptide, that binds to the liganded receptor in an AF2-independent manner. The 2-A, crystal structure of the ER/peptide complex reveals a binding site that is, centered on a shallow depression on the beta-hairpin face of the, ligand-binding domain. The peptide binds in an unusual extended, conformation and makes multiple contacts with the ligand-binding domain., The location and architecture of the binding site provides an insight into, the peptide's ER subtype specificity and ligand interaction preferences., In vivo, an ... [(full description)]

About this Structure

2BJ4 is a [Single protein] structure of sequence from [Homo sapiens] with OHT as [ligand]. Full crystallographic information is available from [OCA].

Reference

Delineation of a unique protein-protein interaction site on the surface of the estrogen receptor., Kong EH, Heldring N, Gustafsson JA, Treuter E, Hubbard RE, Pike AC, Proc Natl Acad Sci U S A. 2005 Mar 8;102(10):3593-8. Epub 2005 Feb 23. PMID:15728727

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