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Crystal structure of protein C inhibitor provides insights into hormone binding and heparin activation

In English

Författare

Summary, in English

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 Angstrom 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.

Publiceringsår

2003

Språk

Engelska

Sidor

205-215

Publikation/Tidskrift/Serie

Structure

Volym

11

Issue

2

Dokumenttyp

Artikel i tidskrift

Förlag

Cell Press

Ämne

  • Medicinal Chemistry

Status

Published

Forskningsgrupp

  • Clinical Chemistry, Malmö

ISBN/ISSN/Övrigt

  • ISSN: 0969-2126