1C9Q

AVERAGE NMR SOLUTION STRUCTURE OF THE BIR-2 DOMAIN OF XIAP

1C9Q の概要

• エントリーDOI: 10.2210/pdb1c9q/pdb
• 分子名称: APOPTOSIS INHIBITOR IAP HOMOLOG, ZINC ION (2 entities in total)
• 機能のキーワード: zinc finger, apoptosis, inhibitor
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P98170
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13645.52

構造登録者

Meadows, R.P.,Fesik, S.W. (登録日: 1999-08-03, 公開日: 2000-08-09, 最終更新日: 2024-05-22)

主引用文献

Sun, C.,Cai, M.,Gunasekera, A.H.,Meadows, R.P.,Wang, H.,Chen, J.,Zhang, H.,Wu, W.,Xu, N.,Ng, S.C.,Fesik, S.W.
NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP.
Nature, 401:818-822, 1999

PubMed Abstract: The inhibitor-of-apoptosis (IAP) family of proteins, originally identified in baculoviruses, regulate programmed cell death in a variety of organisms. IAPs inhibit specific enzymes (caspases) in the death cascade and contain one to three modules of a common 70-amino-acid motif called the BIR domain. Here we describe the nuclear magnetic resonance structure of a region encompassing the second BIR domain (BIR2) of a human IAP family member, XIAP (also called hILP or MIHA). The structure of the BIR domain consists of a three-stranded antiparallel beta-sheet and four alpha-helices and resembles a classical zinc finger. Unexpectedly, conserved amino acids within the linker region between the BIR1 and BIR2 domains were found to be critical for inhibiting caspase-3. The absence or presence of these residues may explain the differences in caspase inhibition observed for different truncated and full-length IAPs. Our data further indicate that these residues may bind to the active site and that the BIR domain may interact with an adjacent site on the enzyme.

PubMed: 10548111
DOI: 10.1038/44617

実験手法

SOLUTION NMR