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1szh
From Proteopedia
(New page: 200px<br /><applet load="1szh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1szh, resolution 1.50Å" /> '''Crystal Structure of...) |
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| - | [[Image:1szh.gif|left|200px]]<br /><applet load="1szh" size=" | + | [[Image:1szh.gif|left|200px]]<br /><applet load="1szh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1szh, resolution 1.50Å" /> | caption="1szh, resolution 1.50Å" /> | ||
'''Crystal Structure of C. elegans HER-1'''<br /> | '''Crystal Structure of C. elegans HER-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | HER-1 is a secreted protein that promotes male development in the nematode | + | 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== | ==About this Structure== | ||
| - | 1SZH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] with ACT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1SZH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans] with <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SZH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Caenorhabditis elegans]] | [[Category: Caenorhabditis elegans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Geisbrecht, B | + | [[Category: Geisbrecht, B V.]] |
| - | [[Category: Hamaoka, B | + | [[Category: Hamaoka, B Y.]] |
| - | [[Category: III, C | + | [[Category: III, C E.Dann.]] |
| - | [[Category: Leahy, D | + | [[Category: Leahy, D J.]] |
[[Category: ACT]] | [[Category: ACT]] | ||
[[Category: extended 3-10 helix; left-handed anti-parallel 4-helix bundle]] | [[Category: extended 3-10 helix; left-handed anti-parallel 4-helix bundle]] | ||
[[Category: overhand 3-helix bundle]] | [[Category: overhand 3-helix bundle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:07:50 2008'' |
Revision as of 13:07, 21 February 2008
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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 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
Page seeded by OCA on Thu Feb 21 15:07:50 2008
