Abstract
Survivin is a mitotic spindle-associated protein involved in linking mitotic spindle function to activation of apoptosis in mammalian cells. The structure of the full-length human survivin has been determined by X-ray crystallography to 2.7 A. Strikingly, the structure forms a very unusual bow tie-shaped dimer. It does not dimerize through a C-terminal coiled-coil, contrary to sequence analysis prediction. The C-terminal helices contain hydrophobic clusters with the potential for protein-protein interactions. The unusual shape and dimensions of survivin suggest it serves an adaptor function through its alpha-helical extensions.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Apoptosis / physiology
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Crystallography, X-Ray
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Dimerization
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Humans
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Inhibitor of Apoptosis Proteins
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Microtubule-Associated Proteins*
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Models, Molecular
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Molecular Sequence Data
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Neoplasm Proteins
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Protein Structure, Quaternary
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Proteins / chemistry*
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Proteins / genetics
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Proteins / physiology
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Sequence Homology, Amino Acid
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Survivin
Substances
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BIRC5 protein, human
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Inhibitor of Apoptosis Proteins
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Microtubule-Associated Proteins
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Neoplasm Proteins
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Proteins
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Recombinant Proteins
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Survivin