title: X-ray crystallographic studies on fibrinogen and fibrin.
abstract: More than a dozen crystal structures of fibrinogen and fibrin fragments have been reported, including a structure of a native fibrinogen. The majority of the other structures are fragments D and d-dimer crystallized in the presence or absence of synthetic peptide ligands patterned on the A and B 'knobs'. Overall, fibrinogens or their fragments from four different species--human, bovine, chicken and lamprey--have been studied so far, with only minor differences in the structures being observed. Although these studies have thrown much light on the details of the fibrinogen to fibrin conversion, much remains to be found out.
authors.affiliation: Center for Molecular Genetics, University of California, San Diego, La Jolla, California 92093-0634, USA. rdoolittle@ucsd.edu
authors.forename: R F
authors.initials: RF
authors.lastname: Doolittle
mesh_terms: D000818:Animals; D002417:Cattle; D002645:Chickens; D018360:Crystallography, X-Ray; D005337:Fibrin / Q000737:chemistry*; D005340:Fibrinogen / Q000737:chemistry*; D006801:Humans; D007798:Lampreys; D008024:Ligands; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D008024:Ligands; D011994:Recombinant Proteins; D005337:Fibrin; D005340:Fibrinogen