Teruko Sugo, Yoichi Sakata and Michio Matsuda Pages 239 - 247 ( 9 )
Dysfibrinogens can be grossly divided in two groups: (1) defective thrombin-catalyzed conversion of fibrinogen molecules to fibrin monomers, and (2) defective fibrin polymerization due to structural alterations in polymerization sites, that include “A” and “a” sites, end-to-end D:D abutment surfaces, and lateral association sites involving the carboxyl terminal region of the fibrin α-chain. Recently, a number of mutations in the fibrinogen genes have been identified, and many of these encode changes that occur in regions of fibrinogen that have been elucidated by high-resolution structural studies. Here we focus on the structure-function relationships of fibrinogen that can be inferred from studies involving these abnormal molecules.
dysfibrinogens, gamma275, alpha-16, dysfibrogenernias, d:d interface
Division of Cell and Molecular Medicine, Center for Molecular Medicine, Jichi Medical School, Yakushiji 3311-1, Tochigi, 329-0498, Japan