1C9Q
AVERAGE NMR SOLUTION STRUCTURE OF THE BIR-2 DOMAIN OF XIAP
Summary for 1C9Q
| Entry DOI | 10.2210/pdb1c9q/pdb |
| Descriptor | APOPTOSIS INHIBITOR IAP HOMOLOG, ZINC ION (2 entities in total) |
| Functional Keywords | zinc finger, apoptosis, inhibitor |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: P98170 |
| Total number of polymer chains | 1 |
| Total formula weight | 13645.52 |
| Authors | Meadows, R.P.,Fesik, S.W. (deposition date: 1999-08-03, release date: 2000-08-09, Last modification date: 2024-05-22) |
| Primary citation | 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 Cited by 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: 10548111DOI: 10.1038/44617 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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