1e31: Difference between revisions

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[[Image:1e31.gif|left|200px]]
[[Image:1e31.gif|left|200px]]


{{Structure
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{{STRUCTURE_1e31| PDB=1e31  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e31 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e31 OCA], [http://www.ebi.ac.uk/pdbsum/1e31 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e31 RCSB]</span>
}}


'''SURVIVIN DIMER H. SAPIENS'''
'''SURVIVIN DIMER H. SAPIENS'''
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[[Category: Margolis, R.]]
[[Category: Margolis, R.]]
[[Category: Skoufias, D.]]
[[Category: Skoufias, D.]]
[[Category: apotosis]]
[[Category: Apotosis]]
[[Category: iap]]
[[Category: Iap]]
[[Category: zinc finger]]
[[Category: Zinc finger]]
 
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Revision as of 11:35, 2 May 2008

File:1e31.gif

Template:STRUCTURE 1e31

SURVIVIN DIMER H. SAPIENS


Overview

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.

About this Structure

1E31 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 14:35:49 2008

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