1szh
From Proteopedia
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|PDB= 1szh |SIZE=350|CAPTION= <scene name='initialview01'>1szh</scene>, resolution 1.50Å | |PDB= 1szh |SIZE=350|CAPTION= <scene name='initialview01'>1szh</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= HER-1, ZK287.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans]) | |GENE= HER-1, ZK287.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 Caenorhabditis elegans]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1szh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1szh OCA], [http://www.ebi.ac.uk/pdbsum/1szh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1szh RCSB]</span> | ||
}} | }} | ||
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[[Category: III, C E.Dann.]] | [[Category: III, C E.Dann.]] | ||
[[Category: Leahy, D J.]] | [[Category: Leahy, D J.]] | ||
| - | [[Category: | + | [[Category: extended 3-10 helix]] |
| - | [[Category: | + | [[Category: left-handed anti-parallel 4-helix bundle]] |
[[Category: overhand 3-helix bundle]] | [[Category: overhand 3-helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:02 2008'' |
Revision as of 20:49, 30 March 2008
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| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | HER-1, ZK287.8 (Caenorhabditis elegans) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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