The structure-function relationship of hereditary dysfibrinogens.
Fibrinogen is a 340-kDa multi-subunit glycoprotein present in plasma and tissues of all classes of vertebrates. Fibrinogen exerts a variety of physiologically important functions, and most of them, if not all, are assigned to certain structures of fibrin including double-stranded fibrin protofibrils and highly crosslinked fibrin networks. Fibrin formation is indeed a series of highly ordered molecular interactions. The mechanisms underlying these molecular interactions have been extensively studied in the last 40 years, but there still remain many enigmas. In this mini-review, the structure-function relationships of hereditary dysfibrinogens are discussed.
Matsuda
M
M
Division of Hemostasis and Thrombosis Research, Jichi Medical School, Tochigi-Ken, Japan.
D000347:Afibrinogenemia / Q000235:genetics*; D005337:Fibrin / Q000378:metabolism; D005340:Fibrinogen / Q000737:chemistry / Q000502:physiology; D015241:Fibrinogens, Abnormal / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D006801:Humans; D011108:Polymers; D011485:Protein Binding; D013329:Structure-Activity Relationship
D015241:Fibrinogens, Abnormal; D011108:Polymers; D005337:Fibrin; D005340:Fibrinogen