1LQ8: Crystal Structure Of Cleaved Protein C Inhibitor

Citation:
Abstract
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.
PDB ID: 1LQ8Download
MMDB ID: 22007
PDB Deposition Date: 2002/5/9
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Similar Structures:
Biological Unit for 1LQ8: dimeric; determined by author and by software (PISA,PQS)
Molecular Components in 1LQ8
Label Count Molecule
Proteins (2 molecules)
1
Plasma Serine Protease Inhibitor(Gene symbol: SERPINA5)
Molecule annotation
1
Plasma Serine Protease Inhibitor(Gene symbol: SERPINA5)
Molecule annotation
Chemicals (5 molecules)
1
3
2
1
3
1
* Click molecule labels to explore molecular sequence information.

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