1lq8
From Proteopedia
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[[Image:1lq8.gif|left|200px]] | [[Image:1lq8.gif|left|200px]] | ||
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'''Crystal structure of cleaved protein C inhibitor''' | '''Crystal structure of cleaved protein C inhibitor''' | ||
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[[Category: Kjellberg, M.]] | [[Category: Kjellberg, M.]] | ||
[[Category: Stenflo, J.]] | [[Category: Stenflo, J.]] | ||
- | [[Category: | + | [[Category: Heparin]] |
- | [[Category: | + | [[Category: Inhibitor]] |
- | [[Category: | + | [[Category: Protease]] |
- | [[Category: | + | [[Category: Protein c]] |
- | [[Category: | + | [[Category: Retinoic acid]] |
- | [[Category: | + | [[Category: Serpin]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:10:07 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 21:10, 2 May 2008
Crystal structure of cleaved protein C inhibitor
Overview
Protein C inhibitor (PCI) is a member of the serpin family that has many biological functions. In blood it acts as a procoagulant, and, in the seminal vesicles, it is required for spermatogenesis. The activity of PCI is affected by heparin binding in a manner unique among the heparin binding serpins, and, in addition, PCI binds hydrophobic hormones with apparent specificity for retinoids. Here we present the 2.4 A crystallographic structure of reactive center loop (RCL) cleaved PCI. A striking feature of the structure is a two-turn N-terminal shortening of helix A, which creates a large hydrophobic pocket that docking studies indicate to be the retinoid binding site. On the basis of surface electrostatic properties, a novel mechanism for heparin activation is proposed.
About this Structure
1LQ8 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of protein C inhibitor provides insights into hormone binding and heparin activation., Huntington JA, Kjellberg M, Stenflo J, Structure. 2003 Feb;11(2):205-15. PMID:12575940 Page seeded by OCA on Sat May 3 00:10:07 2008