2hew

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(New page: 200px<br /><applet load="2hew" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hew, resolution 1.45&Aring;" /> '''The X-ray crystal st...)
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[[Image:2hew.gif|left|200px]]<br /><applet load="2hew" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2hew.gif|left|200px]]<br /><applet load="2hew" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2hew, resolution 1.45&Aring;" />
caption="2hew, resolution 1.45&Aring;" />
'''The X-ray crystal structure of murine OX40L'''<br />
'''The X-ray crystal structure of murine OX40L'''<br />
==Overview==
==Overview==
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OX40 is a T cell costimulator activated by OX40L. Blockade of the, OX40L-OX40 interaction has ameliorative effects in animal models of T cell, pathologies. In order to better understand the interaction between OX40, and OX40L, we have determined the crystal structure of murine OX40L and of, the human OX40-OX40L complex at 1.45 and 2.4 A, respectively. These, structures show that OX40L is an unusually small member of the tumor, necrosis factor superfamily (TNFSF). The arrangement of the OX40L, protomers forming the functional trimer is atypical and differs from that, of other members by a 15 degrees rotation of each protomer with respect to, the trimer axis, resulting in an open assembly. Site-directed changes of, the interfacial residues of OX40L suggest this interface lacks a single, "hot spot" and that instead, binding energy is dispersed over at least two, distinct areas. These structures demonstrate the structural plasticity of, TNFSF members and their interactions with receptors.
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OX40 is a T cell costimulator activated by OX40L. Blockade of the OX40L-OX40 interaction has ameliorative effects in animal models of T cell pathologies. In order to better understand the interaction between OX40 and OX40L, we have determined the crystal structure of murine OX40L and of the human OX40-OX40L complex at 1.45 and 2.4 A, respectively. These structures show that OX40L is an unusually small member of the tumor necrosis factor superfamily (TNFSF). The arrangement of the OX40L protomers forming the functional trimer is atypical and differs from that of other members by a 15 degrees rotation of each protomer with respect to the trimer axis, resulting in an open assembly. Site-directed changes of the interfacial residues of OX40L suggest this interface lacks a single "hot spot" and that instead, binding energy is dispersed over at least two distinct areas. These structures demonstrate the structural plasticity of TNFSF members and their interactions with receptors.
==About this Structure==
==About this Structure==
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2HEW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with NAG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HEW OCA].
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2HEW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HEW OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Compaan, D.M.]]
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[[Category: Compaan, D M.]]
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[[Category: Hymowitz, S.G.]]
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[[Category: Hymowitz, S G.]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: trimer]]
[[Category: trimer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:42:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:41:10 2008''

Revision as of 15:41, 21 February 2008

Image:2hew.gif

2hew, resolution 1.45Å

Drag the structure with the mouse to rotate

The X-ray crystal structure of murine OX40L

Overview

OX40 is a T cell costimulator activated by OX40L. Blockade of the OX40L-OX40 interaction has ameliorative effects in animal models of T cell pathologies. In order to better understand the interaction between OX40 and OX40L, we have determined the crystal structure of murine OX40L and of the human OX40-OX40L complex at 1.45 and 2.4 A, respectively. These structures show that OX40L is an unusually small member of the tumor necrosis factor superfamily (TNFSF). The arrangement of the OX40L protomers forming the functional trimer is atypical and differs from that of other members by a 15 degrees rotation of each protomer with respect to the trimer axis, resulting in an open assembly. Site-directed changes of the interfacial residues of OX40L suggest this interface lacks a single "hot spot" and that instead, binding energy is dispersed over at least two distinct areas. These structures demonstrate the structural plasticity of TNFSF members and their interactions with receptors.

About this Structure

2HEW is a Single protein structure of sequence from Mus musculus with and as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of the costimulatory OX40-OX40L complex., Compaan DM, Hymowitz SG, Structure. 2006 Aug;14(8):1321-30. PMID:16905106

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