2hey: Difference between revisions

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[[Image:2hey.~~gif~~|left|200px]]

[[Image:2hey.png|left|200px]]

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~~'''~~Crystal structure of murine OX40L bound to human OX40~~'''~~

===Crystal structure of murine OX40L bound to human OX40===

~~==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.

The line below this paragraph, {{ABSTRACT_PUBMED_16905106}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16905106 is the PubMed ID number.

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==About this Structure==

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[[Category: Receptor-ligan complex]]

[[Category: Tnfsf]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun ~~May 4 06~~:12~~:49~~ 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:48:12 2008''

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-[[Image:2hey.gif|left|200px]]
+{{Seed}}
+[[Image:2hey.png|left|200px]]
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 {{STRUCTURE_2hey|  PDB=2hey  |  SCENE=  }}
-'''Crystal structure of murine OX40L bound to human OX40'''
+===Crystal structure of murine OX40L bound to human OX40===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16905106}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16905106 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16905106}}
 ==About this Structure==
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 [[Category: Receptor-ligan complex]]
 [[Category: Tnfsf]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:12:49 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:48:12 2008''