1lq8
From Proteopedia
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Crystal structure of cleaved protein C inhibitor
Contents |
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.
Disease
Known diseases associated with this structure: Protein C inhibitor deficiency OMIM:[601841]
About this Structure
1LQ8 is a Protein complex structure of sequences from Homo sapiens with NDG and IPA as ligands. 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 Mon Nov 12 18:03:29 2007
Categories: Homo sapiens | Protein complex | Huntington, J.A. | Kjellberg, M. | Stenflo, J. | IPA | NDG | Heparin | Inhibitor | Protease | Protein c | Retinoic acid | Serpin
