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