1e31: Difference between revisions
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[[Image:1e31.gif|left|200px]] | [[Image:1e31.gif|left|200px]] | ||
'''SURVIVIN DIMER H. SAPIENS''' | {{Structure | ||
|PDB= 1e31 |SIZE=350|CAPTION= <scene name='initialview01'>1e31</scene>, resolution 2.71Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=CO:COBALT (II) ION'>CO</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''SURVIVIN DIMER H. SAPIENS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1E31 is a [ | 1E31 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E31 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10949039 10949039] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:48:44 2008'' | ||
Revision as of 08:48, 20 March 2008
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| 1e31, resolution 2.71Å | |||||||||||||
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| Ligands: | ZN and CO | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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