Abstract
Recent X-ray crystallography studies on fragments D and DD from fibrinogen and fibrin have revealed the nature of the interaction at the ends of the individual fibrin units. Additionally, cocrystallization of fragments with synthetic peptides patterned on the sequences exposed by the thrombin-catalyzed removal of the fibrinopeptides has provided the details of knob-hole interactions. Interestingly, fragments complexed with the synthetic peptide corresponding to the B knob (GHRPam) exhibit a large conformational change in the presence of the ligand, adding to the intrigue of the still not well understood role of fibrinopeptide B removal.
