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1szh

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(New page: 200px<br /><applet load="1szh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1szh, resolution 1.50&Aring;" /> '''Crystal Structure of...)
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Revision as of 00:45, 21 November 2007


1szh, resolution 1.50Å

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Crystal Structure of C. elegans HER-1

Overview

HER-1 is a secreted protein that promotes male development in the nematode, Caenorhabditis elegans. HER-1 inhibits the function of TRA-2A, a multipass, integral membrane protein thought to serve as its receptor. We report here, the 1.5-A crystal structure of HER-1. The structure was solved by the, multiwavelength anomalous diffraction method by using, selenomethionyl-substituted HER-1 produced in Chinese hamster ovary cells., The HER-1 structure consists of two all-helical domains and is not closely, homologous to any known structure. Sites of amino acid substitutions known, to impair HER-1 function were mapped on the HER-1 structure and classified, according to the likely mechanism by which they affect HER-1 activity. A, subset of these and other amino acid substitutions on the HER-1 surface, were assayed for their ability to disrupt interactions between HER-1 and, TRA-2A-expressing cells, and a localized region on the HER-1 surface, important for mediating this interaction was identified.

About this Structure

1SZH is a Single protein structure of sequence from Caenorhabditis elegans with ACT as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of Caenorhabditis elegans HER-1 and characterization of the interaction between HER-1 and TRA-2A., Hamaoka BY, Dann CE 3rd, Geisbrecht BV, Leahy DJ, Proc Natl Acad Sci U S A. 2004 Aug 10;101(32):11673-8. Epub 2004 Aug 2. PMID:15289613

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