3M0D

Crystal structure of the TRAF1:TRAF2:cIAP2 complex

Summary for 3M0D

• Entry DOI: 10.2210/pdb3m0d/pdb
• Related: 3M06 3M0A
• Descriptor: TNF receptor-associated factor 2, TNF receptor-associated factor 1, Baculoviral IAP repeat-containing protein 3, ... (5 entities in total)
• Functional Keywords: trimeric helix coiled coiled, acetylation, alternative splicing, apoptosis, coiled coil, cytoplasm, metal-binding, ubl conjugation, polymorphism, chromosomal rearrangement, signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q12933; Cytoplasm (Potential): Q13489
• Total number of polymer chains: 4
• Total formula weight: 31261.29

Authors

Kabaleeswaran, V.,Wu, H. (deposition date: 2010-03-02, release date: 2010-04-28, Last modification date: 2023-09-06)

Primary citation

Zheng, C.,Kabaleeswaran, V.,Wang, Y.,Cheng, G.,Wu, H.
Crystal structures of the TRAF2: cIAP2 and the TRAF1: TRAF2: cIAP2 complexes: affinity, specificity, and regulation.
Mol.Cell, 38:101-113, 2010

PubMed 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.

PubMed: 20385093
DOI: 10.1016/j.molcel.2010.03.009

Experimental method

X-RAY DIFFRACTION (2.8 Å)