3m1d is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Asymmetric recruitment of cIAPs by TRAF2.,Mace PD, Smits C, Vaux DL, Silke J, Day CL J Mol Biol. 2010 Jul 2;400(1):8-15. Epub 2010 May 4. PMID:20447407[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Mace PD, Smits C, Vaux DL, Silke J, Day CL. Asymmetric recruitment of cIAPs by TRAF2. J Mol Biol. 2010 Jul 2;400(1):8-15. Epub 2010 May 4. PMID:20447407 doi:10.1016/j.jmb.2010.04.055
