3M1D

Structure of BIR1 from cIAP1

Summary for 3M1D

• Entry DOI: 10.2210/pdb3m1d/pdb
• Descriptor: Baculoviral IAP repeat-containing protein 2, ZINC ION (3 entities in total)
• Functional Keywords: bir, iap, apoptosis, zinc-finger, metal binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q13490
• Total number of polymer chains: 2
• Total formula weight: 19126.60

Authors

Mace, P.D.,Day, C.L. (deposition date: 2010-03-04, release date: 2010-05-26, Last modification date: 2024-11-13)

Primary citation

Mace, P.D.,Smits, C.,Vaux, D.L.,Silke, J.,Day, C.L.
Asymmetric recruitment of cIAPs by TRAF2
J.Mol.Biol., 400:8-15, 2010

PubMed Abstract: Cellular inhibitor of apoptosis protein (cIAP) 1 and cIAP2 set the balance between transcription factor and apoptosis signaling downstream of tumor necrosis factor (TNF) receptor superfamily members by acting as ubiquitin E3 ligases for substrates that are part of the TNF receptor complex. To fulfill this role, cIAPs must be recruited to the receptor complex by TNF-receptor-associated factor (TRAF) 2. In this study, we reconstituted the complex between baculoviral IAP repeat (BIR) 1 of cIAP1 and the coiled-coil region of TRAF2, solved the structure of BIR1 from cIAP1, and mapped key binding residues on each molecule using mutagenesis. Biophysical analysis indicates that a single BIR1 domain binds the trimeric TRAF2 coiled-coil domain. This suggests that only one IAP molecule binds to each TRAF trimer and makes it likely that the dimeric cIAPs crosslink two TRAF trimers.

PubMed: 20447407
DOI: 10.1016/j.jmb.2010.04.055

Experimental method

X-RAY DIFFRACTION (2 Å)