Blood coagulation: The outstanding hydrophobic residues

Curr Biol. 2000 Mar 23;10(6):R237-40. doi: 10.1016/s0960-9822(00)00373-0.

Abstract

Newly determined crystal structures suggest that the membrane-binding C2 domains of blood coagulation cofactors Va and VIIIa bind anionic phospholipids through protruding solvent-exposed hydrophobic residues, aided by a crown of positively charged residues and by specific hydrogen-bonding side chains.

Publication types

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

MeSH terms

  • Binding Sites
  • Blood Coagulation
  • Factor VIIIa / genetics
  • Factor VIIIa / metabolism*
  • Factor Va / genetics
  • Factor Va / metabolism*
  • Humans
  • Mutagenesis
  • Phospholipids / metabolism*

Substances

  • Phospholipids
  • Factor Va
  • Factor VIIIa