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1lq8
From Proteopedia
| 1lq8, resolution 2.40Å () | |||||||||
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| Ligands: | , | ||||||||
| Non-Standard Residues: | , | ||||||||
| Domains: | alpha-1-antitrypsin_like | ||||||||
| Related: | 1ezx | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Crystal structure of cleaved protein C inhibitor
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1LQ8 is a 8 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Huntington JA, Kjellberg M, Stenflo J. Crystal structure of protein C inhibitor provides insights into hormone binding and heparin activation. Structure. 2003 Feb;11(2):205-15. PMID:12575940
Page seeded by OCA on Wed Feb 18 06:14:33 2009
Categories: Homo sapiens | Huntington, J A. | Kjellberg, M. | Stenflo, J. | Heparin | Inhibitor | Protease | Protein c | Retinoic acid | Serpin
