2hey: Difference between revisions

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New page: left|200px<br /> <applet load="2hey" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hey, resolution 2.00Å" /> '''Crystal structure o...
 
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[[Image:2hey.gif|left|200px]]<br />
[[Image:2hey.gif|left|200px]]<br /><applet load="2hey" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2hey" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2hey, resolution 2.00&Aring;" />
caption="2hey, resolution 2.00&Aring;" />
'''Crystal structure of murine OX40L bound to human OX40'''<br />
'''Crystal structure of murine OX40L bound to human OX40'''<br />


==Overview==
==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.
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==
2HEY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HEY OCA].  
2HEY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HEY OCA].  


==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Hymowitz, S.G.]]
[[Category: Hymowitz, S G.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: co-stimulator]]
[[Category: co-stimulator]]
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[[Category: tnfsf]]
[[Category: tnfsf]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:31:46 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:41:16 2008''

Revision as of 18:41, 21 February 2008

File:2hey.gif


2hey, resolution 2.00Å

Drag the structure with the mouse to rotate

Crystal structure of murine OX40L bound to human OX40

OverviewOverview

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 StructureAbout this Structure

2HEY is a Protein complex structure of sequences from Homo sapiens and Mus musculus with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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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