NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP (Q27620280)

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A H Gunasekera

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R P Meadows

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H Wang

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J Chen

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H Zhang

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W Wu

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N Xu

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S C Ng

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S W Fesik

An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif

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language of work or name

English

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publication date

21 October 1999

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published in

Nature

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volume

401

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issue

6755

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page(s)

818-22

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cites work

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Drosophila homologs of baculovirus inhibitor of apoptosis proteins function to block cell death

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The gene for neuronal apoptosis inhibitory protein is partially deleted in individuals with spinal muscular atrophy

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A conserved family of cellular genes related to the baculovirus iap gene and encoding apoptosis inhibitors

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Cloning and expression of apoptosis inhibitory protein homologs that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors

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A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma

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Inhibition of interleukin 1 beta-converting enzyme-mediated apoptosis of mammalian cells by baculovirus IAP.

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X-linked IAP is a direct inhibitor of cell-death proteases

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The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases

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A single BIR domain of XIAP sufficient for inhibiting caspases

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Conservation of baculovirus inhibitor of apoptosis repeat proteins (BIRPs) in viruses, nematodes, vertebrates and yeasts.

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Zinc mining for protein domains

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Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions

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A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis

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The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis

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Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat

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Multidimensional heteronuclear nuclear magnetic resonance of proteins

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Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling

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Protein backbone angle restraints from searching a database for chemical shift and sequence homology

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Torsion-angle molecular dynamics as a new efficient tool for NMR structure calculation.

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Determination of three-dimensional structures of proteins by simulated annealing with interproton distance restraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2.

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Use of dipolar 1H-15N and 1H-13C couplings in the structure determination of magnetically oriented macromolecules in solution

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Sensitivity improvement of transverse relaxation-optimized spectroscopy

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Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

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