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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2000-8-31
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
183-9
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10949039-Amino Acid Sequence,
pubmed-meshheading:10949039-Apoptosis,
pubmed-meshheading:10949039-Crystallography, X-Ray,
pubmed-meshheading:10949039-Dimerization,
pubmed-meshheading:10949039-Humans,
pubmed-meshheading:10949039-Inhibitor of Apoptosis Proteins,
pubmed-meshheading:10949039-Microtubule-Associated Proteins,
pubmed-meshheading:10949039-Models, Molecular,
pubmed-meshheading:10949039-Molecular Sequence Data,
pubmed-meshheading:10949039-Neoplasm Proteins,
pubmed-meshheading:10949039-Protein Structure, Quaternary,
pubmed-meshheading:10949039-Protein Structure, Secondary,
pubmed-meshheading:10949039-Protein Structure, Tertiary,
pubmed-meshheading:10949039-Proteins,
pubmed-meshheading:10949039-Recombinant Proteins,
pubmed-meshheading:10949039-Sequence Homology, Amino Acid
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pubmed:year |
2000
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pubmed:articleTitle |
Crystal structure of human survivin reveals a bow tie-shaped dimer with two unusual alpha-helical extensions.
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pubmed:affiliation |
Laboratoire de Cristallographie Macromoléculaire, Institut de Biologie Structurale Jean-Pierre Ebel, CEA-CNRS, Grenoble, France.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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