1qsc

From Proteopedia

Revision as of 16:49, 12 November 2007

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 with ACE as ligand. 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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