1e31 | pdb_00001e31
From Proteopedia
SURVIVIN DIMER H. SAPIENS
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Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSurvivin 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. Crystal structure of human survivin reveals a bow tie-shaped dimer with two unusual alpha-helical extensions.,Chantalat L, Skoufias DA, Kleman JP, Jung B, Dideberg O, Margolis RL Mol Cell. 2000 Jul;6(1):183-9. PMID:10949039[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References | ||||||||||||||||||
This page was last modified 07:56, 13 December 2017.