title: Human fibrinogen: anticipating a 3-dimensional structure.
abstract: The principal component of blood clots is a protein meshwork called fibrin. The precursor protein, fibrinogen, occurs in a soluble form in the blood plasma where it is activated by thrombin when and if the need arises. More than a century after first being purified, fibrinogen has yet to have its detailed 3-dimensional structure revealed. The situation is changing rapidly, however, and crystallographic studies in progress in several laboratories on a variety of fragments and complexes may soon reveal not only its structure but also the subtleties of how this large glycoprotein is transformed into a fibrin clot.
authors.affiliation: Center for Molecular Genetics, University of California, San Diego, La Jolla 92093-0634, USA.
authors.forename: R F
authors.initials: RF
authors.lastname: Doolittle
authors.forename: S J
authors.initials: SJ
authors.lastname: Everse
authors.forename: G
authors.initials: G
authors.lastname: Spraggon
mesh_terms: D001777:Blood Coagulation / Q000502:physiology; D018360:Crystallography, X-Ray; D005340:Fibrinogen / Q000737:chemistry* / Q000502:physiology; D006801:Humans; D009842:Oligopeptides / Q000737:chemistry; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D009842:Oligopeptides; D011994:Recombinant Proteins; C035024:glycyl-prolyl-arginine; D005340:Fibrinogen