1szh: Difference between revisions

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[[Image:1szh.gif|left|200px]]<br /><applet load="1szh" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1szh.gif|left|200px]]<br /><applet load="1szh" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1szh, resolution 1.50Å" />

'''Crystal Structure of C. elegans HER-1'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1SZH OCA].

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==

Line 13:

[[Category: Caenorhabditis elegans]]

[[Category: Single protein]]

[[Category: Geisbrecht, B.V.]]

[[Category: Geisbrecht, B V.]]

[[Category: Hamaoka, B.Y.]]

[[Category: Hamaoka, B Y.]]

[[Category: III, C.E.Dann.]]

[[Category: III, C E.Dann.]]

[[Category: Leahy, D.J.]]

[[Category: Leahy, D J.]]

[[Category: ACT]]

[[Category: extended 3-10 helix; left-handed anti-parallel 4-helix bundle]]

[[Category: overhand 3-helix bundle]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 02:52:~~21 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:07:50 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1szh.gif|left|200px]]<br /><applet load="1szh" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1szh.gif|left|200px]]<br /><applet load="1szh" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1szh, resolution 1.50&Aring;" />
 '''Crystal Structure of C. elegans HER-1'''<br />
 ==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.
+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==
-SZH 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SZH OCA].
+SZH 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==
@@ Line 13: / Line 13: @@
 [[Category: Caenorhabditis elegans]]
 [[Category: Single protein]]
-[[Category: Geisbrecht, B.V.]]
+[[Category: Geisbrecht, B V.]]
-[[Category: Hamaoka, B.Y.]]
+[[Category: Hamaoka, B Y.]]
-[[Category: III, C.E.Dann.]]
+[[Category: III, C E.Dann.]]
-[[Category: Leahy, D.J.]]
+[[Category: Leahy, D J.]]
 [[Category: ACT]]
 [[Category: extended 3-10 helix; left-handed anti-parallel 4-helix bundle]]
 [[Category: overhand 3-helix bundle]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:52:21 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:07:50 2008''