1e31: Difference between revisions

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[[Image:1e31.gif|left|200px]]
{{Seed}}
[[Image:1e31.png|left|200px]]


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{{STRUCTURE_1e31|  PDB=1e31  |  SCENE=  }}  
{{STRUCTURE_1e31|  PDB=1e31  |  SCENE=  }}  


'''SURVIVIN DIMER H. SAPIENS'''
===SURVIVIN DIMER H. SAPIENS===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_10949039}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10949039 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10949039}}


==About this Structure==
==About this Structure==
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[[Category: Iap]]
[[Category: Iap]]
[[Category: Zinc finger]]
[[Category: Zinc finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:03:53 2008''

Revision as of 21:03, 30 June 2008

File:1e31.png

Template:STRUCTURE 1e31

SURVIVIN DIMER H. SAPIENS

Template:ABSTRACT PUBMED 10949039

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

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