Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin

Nature. 1997 Oct 2;389(6650):455-62. doi: 10.1038/38947.

Abstract

In blood coagulation, units of the protein fibrinogen pack together to form a fibrin clot, but a crystal structure for fibrinogen is needed to understand how this is achieved. The structure of a core fragment (fragment D) from human fibrinogen has now been determined to 2.9 A resolution. The 86K three-chained structure consists of a coiled-coil region and two homologous globular entitles oriented at approximately 130 degrees to each other. Additionally, the covalently bound dimer of fragment D, known as 'double-D', was isolated from human fibrin, crystallized in the presence of a Gly-Pro-Arg-Pro-amide peptide ligand, which simulates the donor polymerization site, and its structure solved by molecular replacement with the model of fragment D.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Cross-Linking Reagents
  • Crystallography, X-Ray
  • Fibrin / chemistry*
  • Fibrin Fibrinogen Degradation Products / chemistry*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Fragments
  • Protein Conformation*

Substances

  • Cross-Linking Reagents
  • Fibrin Fibrinogen Degradation Products
  • Peptide Fragments
  • fibrinogen D fragment
  • Fibrin

Associated data

  • PDB/1FZA
  • PDB/1FZB