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PDBsum entry 3m06

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protein Protein-protein interface(s) links
Protein binding PDB id
3m06
Jmol
Contents
Protein chains
(+ 0 more) 62 a.a. *
Waters ×61
* Residue conservation analysis
PDB id:
3m06
Name: Protein binding
Title: Crystal structure of traf2
Structure: Tnf receptor-associated factor 2. Chain: a, b, c, d, e, f. Fragment: residues 266-329. Synonym: tumor necrosis factor type 2 receptor-associated p engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: traf2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.67Å     R-factor:   0.194     R-free:   0.233
Authors: V.Kabaleeswaran,H.Wu
Key ref: C.Zheng et al. (2010). Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation. Mol Cell, 38, 101-113. PubMed id: 20385093
Date:
02-Mar-10     Release date:   28-Apr-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q12933  (TRAF2_HUMAN) -  TNF receptor-associated factor 2
Seq:
Struc:
501 a.a.
62 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     regulation of apoptotic process   5 terms 
  Biochemical function     ubiquitin-protein ligase activity     1 term  

 

 
Mol Cell 38:101-113 (2010)
PubMed id: 20385093  
 
 
Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation.
C.Zheng, V.Kabaleeswaran, Y.Wang, G.Cheng, H.Wu.
 
  ABSTRACT  
 
TRAF1/2 and cIAP1/2 are members of the TNF receptor-associated factor (TRAF) and the inhibitor of apoptosis (IAP) families, respectively. They are critical for canonical and noncanonical NF-kappaB signaling pathways. Here, we report the crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes. A TRAF2 trimer interacts with one cIAP2 both in the crystal and in solution. Two chains of the TRAF2 trimer directly contact cIAP2, and key residues at the interface are confirmed by mutagenesis. TRAF1 and TRAF2 preferentially form the TRAF1: (TRAF2)(2) heterotrimer, which interacts with cIAP2 more strongly than TRAF2 alone. In contrast, TRAF1 alone interacts very weakly with cIAP2. Surprisingly, TRAF1 and one chain of TRAF2 in the TRAF1: (TRAF2)(2): cIAP2 ternary complex mediate interaction with cIAP2. Because TRAF1 is upregulated by many stimuli, it may modulate the interaction of TRAF2 with cIAP1/2, which explains regulatory roles of TRAF1 in TNF signaling.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21135870 C.Zheng, Q.Yin, and H.Wu (2011).
Structural studies of NF-κB signaling.
  Cell Res, 21, 183-195.  
21660053 H.Häcker, P.H.Tseng, and M.Karin (2011).
Expanding TRAF function: TRAF3 as a tri-faced immune regulator.
  Nat Rev Immunol, 11, 457-468.  
21232017 H.Wajant, and P.Scheurich (2011).
TNFR1-induced activation of the classical NF-κB pathway.
  FEBS J, 278, 862-876.  
21232018 M.A.O'Donnell, and A.T.Ting (2011).
RIP1 comes back to life as a cell death regulator in TNFR1 signaling.
  FEBS J, 278, 877-887.  
21300983 S.Gardam, V.M.Turner, H.Anderton, S.Limaye, A.Basten, F.Koentgen, D.L.Vaux, J.Silke, and R.Brink (2011).
Deletion of cIAP1 and cIAP2 in murine B lymphocytes constitutively activates cell survival pathways and inactivates the germinal center response.
  Blood, 117, 4041-4051.  
21048983 D.B.Conze, Y.Zhao, and J.D.Ashwell (2010).
Non-canonical NF-κB activation and abnormal B cell accumulation in mice expressing ubiquitin protein ligase-inactive c-IAP2.
  PLoS Biol, 8, e1000518.  
20651737 M.Gyrd-Hansen, and P.Meier (2010).
IAPs: from caspase inhibitors to modulators of NF-kappaB, inflammation and cancer.
  Nat Rev Cancer, 10, 561-574.  
20817427 P.D.Mace, and S.J.Riedl (2010).
Molecular cell death platforms and assemblies.
  Curr Opin Cell Biol, 22, 828-836.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.