1fll
From Proteopedia
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MOLECULAR BASIS FOR CD40 SIGNALING MEDIATED BY TRAF3
Contents |
Overview
Tumor necrosis factor receptors (TNFR) are single transmembrane-spanning, glycoproteins that bind cytokines and trigger multiple signal transduction, pathways. Many of these TNFRs rely on interactions with TRAF proteins that, bind to the intracellular domain of the receptors. CD40 is a member of the, TNFR family that binds to several different TRAF proteins. We have, determined the crystal structure of a 20-residue fragment from the, cytoplasmic domain of CD40 in complex with the TRAF domain of TRAF3. The, CD40 fragment binds as a hairpin loop across the surface of the TRAF, domain. Residues shown by mutagenesis and deletion analysis to be critical, for TRAF3 binding are involved either in direct contact with TRAF3 or in, intramolecular interactions that stabilize the hairpin. Comparison of the, interactions of CD40 with TRAF3 vs. TRAF2 suggests that CD40 may assume, different conformations when bound to different TRAF family members. This, molecular adaptation may influence binding affinity and specific cellular, triggers.
Disease
Known disease associated with this structure: Immunodeficiency with hyper-IgM, type 3 OMIM:[109535]
About this Structure
1FLL is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Molecular basis for CD40 signaling mediated by TRAF3., Ni CZ, Welsh K, Leo E, Chiou CK, Wu H, Reed JC, Ely KR, Proc Natl Acad Sci U S A. 2000 Sep 12;97(19):10395-9. PMID:10984535
Page seeded by OCA on Fri Feb 15 15:48:11 2008
