2qra
From Proteopedia
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Crystal structure of XIAP BIR1 domain (P21 form)
Overview
X-linked inhibitor of apoptosis (XIAP) is a potent negative regulator of, apoptosis. It also plays a role in BMP signaling, TGF-beta signaling, and, copper homeostasis. Previous structural studies have shown that the, baculoviral IAP repeat (BIR2 and BIR3) domains of XIAP interact with the, IAP-binding-motifs (IBM) in several apoptosis proteins such as Smac and, caspase-9 via the conserved IBM-binding groove. Here, we report the, crystal structure in two crystal forms of the BIR1 domain of XIAP, which, does not possess this IBM-binding groove and cannot interact with Smac or, caspase-9. Instead, the BIR1 domain forms a conserved dimer through the, region corresponding to the IBM-binding groove. Structural and sequence, analyses suggest that this dimerization of BIR1 in XIAP may be conserved, in other IAP family members such as cIAP1 and cIAP2 and may be important, for the action of XIAP in TGF-beta and BMP signaling and the action of, cIAP1 and cIAP2 in TNF receptor signaling.
About this Structure
2QRA is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal Structure of the BIR1 Domain of XIAP in Two Crystal Forms., Lin SC, Huang Y, Lo YC, Lu M, Wu H, J Mol Biol. 2007 Sep 28;372(4):847-54. Epub 2007 Jul 21. PMID:17698078
Page seeded by OCA on Wed Jan 23 12:06:40 2008
Categories: Homo sapiens | Single protein | Lin, S.C. | EOH | ZN | Apoptosis | Signaling protein | Zinc binding
