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1qsc

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|PDB= 1qsc |SIZE=350|CAPTION= <scene name='initialview01'>1qsc</scene>, resolution 2.400&Aring;
|PDB= 1qsc |SIZE=350|CAPTION= <scene name='initialview01'>1qsc</scene>, resolution 2.400&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
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|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qsc OCA], [http://www.ebi.ac.uk/pdbsum/1qsc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qsc RCSB]</span>
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[[Category: McWhirter, S M.]]
[[Category: McWhirter, S M.]]
[[Category: Pullen, S S.]]
[[Category: Pullen, S S.]]
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[[Category: ACE]]
 
[[Category: adapter protein]]
[[Category: adapter protein]]
[[Category: cd40 receptor]]
[[Category: cd40 receptor]]
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[[Category: traf]]
[[Category: traf]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:42:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:18:16 2008''

Revision as of 20:18, 30 March 2008

Image:1qsc.gif


PDB ID 1qsc

Drag the structure with the mouse to rotate
, resolution 2.400Å
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE TRAF DOMAIN OF TRAF2 IN A COMPLEX WITH A PEPTIDE FROM THE CD40 RECEPTOR


Overview

Tumor necrosis factor receptor superfamily members convey signals that promote diverse cellular responses. Receptor trimerization by extracellular ligands initiates signaling by recruiting members of the tumor necrosis factor receptor-associated factor (TRAF) family of adapter proteins to the receptor cytoplasmic domains. We report the 2.4-A crystal structure of a 22-kDa, receptor-binding fragment of TRAF2 complexed with a functionally defined peptide from the cytoplasmic domain of the CD40 receptor. TRAF2 forms a mushroom-shaped trimer consisting of a coiled coil and a unique beta-sandwich domain. Both domains mediate trimerization. The CD40 peptide binds in an extended conformation with every side chain in contact with a complementary groove on the rim of each TRAF monomer. The spacing between the CD40 binding sites on TRAF2 supports an elegant signaling mechanism in which trimeric, extracellular ligands preorganize the receptors to simultaneously recognize three sites on the TRAF trimer.

About this Structure

1QSC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystallographic analysis of CD40 recognition and signaling by human TRAF2., McWhirter SM, Pullen SS, Holton JM, Crute JJ, Kehry MR, Alber T, Proc Natl Acad Sci U S A. 1999 Jul 20;96(15):8408-13. PMID:10411888

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