Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin.
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.
Spraggon
G
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Center for Molecular Genetics, University of California, San Diego, La Jolla 92093-0634, USA.
Everse
S J
SJ
Doolittle
R F
RF
D000595:Amino Acid Sequence; D003432:Cross-Linking Reagents; D018360:Crystallography, X-Ray; D005337:Fibrin / Q000737:chemistry*; D005338:Fibrin Fibrinogen Degradation Products / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments; D011487:Protein Conformation
D003432:Cross-Linking Reagents; D005338:Fibrin Fibrinogen Degradation Products; D010446:Peptide Fragments; C015214:fibrinogen D fragment; D005337:Fibrin