1D01

STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A HUMAN CD30 PEPTIDE

Summary for 1D01

• Entry DOI: 10.2210/pdb1d01/pdb
• Related: 1CA4 1CA9 1CZY 1D00 1D0A 1D0J
• Descriptor: TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2, CD30 PEPTIDE (3 entities in total)
• Functional Keywords: b-sandwich, protein-peptide complex, apoptosis
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm : Q12933; Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Cytoplasm: P28908
• Total number of polymer chains: 9
• Total formula weight: 116954.75

Authors

Ye, H.,Park, Y.C.,Kreishman, M.,Kieff, E.,Wu, H. (deposition date: 1999-09-07, release date: 2003-12-02, Last modification date: 2024-10-30)

Primary citation

Ye, H.,Park, Y.C.,Kreishman, M.,Kieff, E.,Wu, H.
The structural basis for the recognition of diverse receptor sequences by TRAF2.
Mol.Cell, 4:321-330, 1999

PubMed Abstract: Many members of the tumor necrosis factor receptor (TNFR) superfamily initiate intracellular signaling by recruiting TNFR-associated factors (TRAFs) through their cytoplasmic tails. TRAFs apparently recognize highly diverse receptor sequences. Crystal structures of the TRAF domain of human TRAF2 in complex with peptides from the TNFR family members CD40, CD30, Ox40, 4-1BB, and the EBV oncoprotein LMP1 revealed a conserved binding mode. A major TRAF2-binding consensus sequence, (P/S/A/T)x(Q/E)E, and a minor consensus motif, PxQxxD, can be defined from the structural analysis, which encompass all known TRAF2-binding sequences. The structural information provides a template for the further dissection of receptor binding specificity of TRAF2 and for the understanding of the complexity of TRAF-mediated signal transduction.

PubMed: 10518213
DOI: 10.1016/S1097-2765(00)80334-2

Experimental method

X-RAY DIFFRACTION (2 Å)