1f3h
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(New page: 200px<br /> <applet load="1f3h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f3h, resolution 2.58Å" /> '''X-RAY CRYSTAL STRUC...)
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Revision as of 14:42, 12 November 2007
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X-RAY CRYSTAL STRUCTURE OF THE HUMAN ANTI-APOPTOTIC PROTEIN SURVIVIN
Overview
Survivin is a 16.5 kDa protein that is expressed during the G2/M phase of, the cell cycle and is hypothesized to inhibit a default apoptotic cascade, initiated in mitosis. This inhibitory function is coupled to survivin's, localization to the mitotic spindle. To begin to address the structural, basis of survivin's function, we report the X-ray crystal structure of a, recombinant form of full length survivin to 2.58 A resolution. Survivin, consists of two defined domains including an N-terminal Zn2+-binding BIR, domain linked to a 65 A amphipathic C-terminal alpha-helix. The crystal, structure reveals an extensive dimerization interface along a hydrophobic, surface on the BIR domain of each survivin monomer. A basic patch acting, as a sulfate/phosphate-binding module, an acidic cluster projecting off, the BIR domain, and a solvent-accessible hydrophobic surface residing on, the C-terminal amphipathic helix, are suggestive of functional, protein-protein interaction surfaces.
About this Structure
1F3H is a Single protein structure of sequence from Homo sapiens with ZN and SO4 as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the human anti-apoptotic protein survivin reveals a dimeric arrangement., Verdecia MA, Huang H, Dutil E, Kaiser DA, Hunter T, Noel JP, Nat Struct Biol. 2000 Jul;7(7):602-8. PMID:10876248
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