Structural alterations in hereditary dysfibrinogens.
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 alpha-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.
Sugo
Teruko
T
Center for Molecular Medicine, Jichi Medical School, Tochigi, 329-0498, Japan. sugosan@jichi.ac.jp
Sakata
Yoichi
Y
Matsuda
Michio
M
D000347:Afibrinogenemia / Q000235:genetics*; D002118:Calcium / Q000378:metabolism; D015241:Fibrinogens, Abnormal / Q000737:chemistry* / Q000235:genetics; D030342:Genetic Diseases, Inborn; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D015241:Fibrinogens, Abnormal; D002118:Calcium