Crystallization and preliminary crystallographic characterization of three peptidic inhibitors in complex with α-thrombin

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt 1):54-8. doi: 10.1107/S1744309110043472. Epub 2010 Dec 21.

Abstract

The serine protease thrombin plays a major role in thrombosis and haemostasis. This has driven interest in thrombin inhibitors as potential antithrombotic drugs. Here, the crystallization and preliminary crystallographic analysis of human α-thrombin in complex with three noncovalent peptide inhibitors of the general sequence D-Phe-Pro-D-Arg-P1'-CONH2 are reported. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1) and diffracted to beyond 1.3 Å resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Peptides / chemistry*
  • Peptides / genetics
  • Serine Proteinase Inhibitors / chemistry*
  • Thrombin / antagonists & inhibitors*
  • Thrombin / chemistry*
  • Thrombin / genetics

Substances

  • Peptides
  • Serine Proteinase Inhibitors
  • Thrombin