Database Accession: DI3000009
Name: TNF receptor associated factor 2 in complex with a peptide from OX40
PDB ID: 1d0a
Experimental method: X-ray (2.00 Å)
Source organism: 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: not assigned
Biological process:
tumor necrosis factor-mediated signaling pathway A series of molecular signals initiated by the binding of a tumor necrosis factor to a receptor on the surface of a cell, and ending with regulation of a downstream cellular process, e.g. transcription.
regulation of apoptotic process Any process that modulates the occurrence or rate of cell death by apoptotic process.
positive regulation of production of molecular mediator of immune response Any process that activates or increases the frequency, rate, or extent of the production of molecular mediator of immune response.
negative regulation of biological process Any process that stops, prevents, or reduces the frequency, rate or extent of a biological process. Biological processes are regulated by many means; examples include the control of gene expression, protein modification or interaction with a protein or substrate molecule.
positive regulation of lymphocyte activation Any process that activates or increases the frequency, rate or extent of lymphocyte activation.
regulation of immunoglobulin secretion Any process that modulates the frequency, rate or extent of the regulated release of immunoglobulins from a cell.
regulation of nucleic acid-templated transcription Any process that modulates the frequency, rate or extent of nucleic acid-templated transcription.
apoptotic signaling pathway A series of molecular signals which triggers the apoptotic death of a cell. The pathway starts with reception of a signal, and ends when the execution phase of apoptosis is triggered.
response to oxygen-containing compound Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an oxygen-containing compound stimulus.
Cellular component:
integral component of plasma membrane The component of the plasma 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: G, A, B, C
Notes: Chains D, E, F, H, I, J, K and L were removed as chains A, B, C and G highlight the biologically relevant interaction.
Name: Tumor necrosis factor receptor superfamily member 4
Source organism: Homo sapiens
Length: 6 residues
Sequence:Sequence according to PDB SEQRESTPIQEE
UniProtKB AC: P43489 (positions: 261-266) Coverage: 2.2%
UniRef90 AC: UniRef90_P43489 (positions: 261-266)
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 G:
The protein region involved in the interaction contains a known functional linear motif (LIG_TRAF2_1).
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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