Database Accession: DI3020001
Name: TNF receptor associated factor 2 in complex with a peptide from LMP1
PDB ID: 1czy
Experimental method: X-ray (2.00 Å)
Source organism: Epstein-Barr virus / Homo sapiens
Proof of disorder:
Primary publication of the structure:
Ye H, Park YC, Kreishman M, Kieff E, Wu H
The structural basis for the recognition of diverse receptor sequences by TRAF2.
(1999) Mol. Cell 4: 321-30
PMID: 10518213
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.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
Biological process:
regulation of protein phosphorylation Any process that modulates the frequency, rate or extent of addition of phosphate groups into an amino acid in a protein.
regulation of cytokine-mediated signaling pathway Any process that modulates the frequency, rate or extent of the cytokine mediated signaling pathway.
regulation of RNA biosynthetic process Any process that modulates the frequency, rate or extent of RNA biosynthetic process.
Cellular component:
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
Structural annotations of the participating protein chains.Entry contents: 4 distinct polypeptide molecules
Chains: D, A, B, C
Notes: Chain E was removed as chains A, B, C and D highlight the biologically relevant interaction.
Name: Latent membrane protein 1
Source organism: Epstein-Barr virus
Length: 7 residues
Sequence:Sequence according to PDB SEQRESPQQATDD
UniProtKB AC: P03230 (positions: 204-210) Coverage: 1.8%
UniRef90 AC: UniRef90_P03230 (positions: 204-210)
Name: TNF receptor-associated factor 2
Source organism: Homo sapiens
Length: 168 residues
Sequence:Sequence according to PDB SEQRESAMADLEQKVLEMEASTYDGVFIWKISDFPRKRQEAVAGRIPAIFSPAFYTSRYGYKMCLRIYLNGDGTGRGTHLSLFFVVMKGPNDALLRWPFNQKVTLMLLDQNNREHVIDAFRPDVTSSSFQRPVNDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIKAIVDLTGL
UniProtKB AC: Q12933 (positions: 334-501) Coverage: 33.5%
UniRef90 AC: UniRef90_Q12933 (positions: 334-501)
Name: TNF receptor-associated factor 2
Source organism: Homo sapiens
Length: 168 residues
Sequence:Sequence according to PDB SEQRESAMADLEQKVLEMEASTYDGVFIWKISDFPRKRQEAVAGRIPAIFSPAFYTSRYGYKMCLRIYLNGDGTGRGTHLSLFFVVMKGPNDALLRWPFNQKVTLMLLDQNNREHVIDAFRPDVTSSSFQRPVNDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIKAIVDLTGL
UniProtKB AC: Q12933 (positions: 334-501) Coverage: 33.5%
UniRef90 AC: UniRef90_Q12933 (positions: 334-501)
Name: TNF receptor-associated factor 2
Source organism: Homo sapiens
Length: 168 residues
Sequence:Sequence according to PDB SEQRESAMADLEQKVLEMEASTYDGVFIWKISDFPRKRQEAVAGRIPAIFSPAFYTSRYGYKMCLRIYLNGDGTGRGTHLSLFFVVMKGPNDALLRWPFNQKVTLMLLDQNNREHVIDAFRPDVTSSSFQRPVNDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIKAIVDLTGL
UniProtKB AC: Q12933 (positions: 334-501) Coverage: 33.5%
UniRef90 AC: UniRef90_Q12933 (positions: 334-501)
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Chain D:
The protein region involved in the interaction contains a known functional linear motif (LIG_TRAF2_2).
Chain A:
The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4.
Chain B:
The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4.
Chain C:
The MATH domain involved in the interaction is known to adopt a stable structure in isolation in trimeric form. A solved structure of the domain trimer without bound ligands is represented by PDB ID 1ca4.
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). No related structure was found in the Protein Data Bank.
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