Calcium-binding site beta 2, adjacent to the "b" polymerization site, modulates lateral aggregation of protofibrils during fibrin polymerization |
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| Authors: | Kostelansky Michael S Lounes Karim C Ping Li Fang Dickerson Sarah K Gorkun Oleg V Lord Susan T |
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| Institution: | Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599-7525, USA. |
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| Abstract: | 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
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