1szh
From Proteopedia
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'''Crystal Structure of C. elegans HER-1''' | '''Crystal Structure of C. elegans HER-1''' | ||
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[[Category: III, C E.Dann.]] | [[Category: III, C E.Dann.]] | ||
[[Category: Leahy, D J.]] | [[Category: Leahy, D J.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:18:43 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:18, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 09:18:43 2008
