fibrinopeptide-a has been researched along with glycylhistidine* in 1 studies
1 other study(ies) available for fibrinopeptide-a and glycylhistidine
| Article | Year |
|---|---|
Calcium-binding site beta 2, adjacent to the "b" polymerization site, modulates lateral aggregation of protofibrils during fibrin polymerization.
Structural analysis of recombinant fibrinogen fragment D revealed that the calcium-binding site (beta2-site) composed of residues BbetaAsp261, BbetaAsp398, BbetaGly263, and gammaGlu132 is modulated by the "B:b" interaction. To determine the beta2-site's role in polymerization, we engineered variant fibrinogen gammaE132A in which calcium binding to the beta2-site was disrupted by replacing glutamic acid at gamma132 with alanine. We compared polymerization of gammaE132A to normal fibrinogen as a function of calcium concentration. Polymerization of gammaE132A at concentrations of calcium Topics: Alanine; Binding Sites; Calcium; Calcium-Binding Proteins; Crystallography, X-Ray; Dipeptides; Fibrin; Fibrin Fibrinogen Degradation Products; Fibrinopeptide A; Fibrinopeptide B; Glutamic Acid; Humans; Mutagenesis, Site-Directed; Protein Binding; Protein Subunits; Recombinant Proteins; Thrombin | 2004 |