title: Blood coagulation: The outstanding hydrophobic residues.
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.
authors.affiliation: Department of Molecular Biology, Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla 92037, USA.
authors.forename: J L
authors.initials: JL
authors.lastname: Pellequer
authors.forename: A J
authors.initials: AJ
authors.lastname: Gale
authors.forename: E D
authors.initials: ED
authors.lastname: Getzoff
mesh_terms: D001665:Binding Sites; D001777:Blood Coagulation; D015944:Factor VIIIa / Q000235:genetics / Q000378:metabolism*; D015943:Factor Va / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D016296:Mutagenesis; D010743:Phospholipids / Q000378:metabolism*
chemical_list: D010743:Phospholipids; D015943:Factor Va; D015944:Factor VIIIa