Abstract
crystallographic 3-D structure of the fibrinogen c chain showsthat the change occurs in an outer region of the molecule(Fig. 1), distant from the two calcium-binding sites of thec chain which are located within the amino acid sequencedefined by residues 311–336 [4]. Moreover, the mutated aminoaciddoesnotliewithintheregionsinvolvedinD–Econtactsites[5]. Taken together, these observations suggest that alteredfibrin polymerization of fibrinogen Vicenza might not beassociated with a direct effect on the sites of interaction withnormal adjacent monomers, but might possibly result fromlong-distanceconformationalchangesinducedbythemutation.References
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