Structure and function of fibrinogen inferred from hereditary dysfibrinogens.
The structure-function relationships of human fibrinogen and their clinical implications are discussed on the basis of data provided by biochemical and electron microscopic analyses of normal and abnormal fibrinogen and by recent crystallographic studies on certain functional domains and segments of normal fibrinogen. Particularly, ultrastructure studies of individual fibrinogen molecules and fibrin networks of structurally elucidated dysfibrinogens enable us to understand the structure-function relationships of these dysfibrinogens more clearly than ever. Electron micrographs of some representative dysfibrinogen molecules are provided.
Matsuda
M
M
Division of Cell and Molecular Medicine, Center for Molecular Medicine, Jichi Medical School, 3311-1 Minamikawachi-Machi, Kawachi-Gun, Tochigi-Ken 329-0498, Japan. thmichi@jichi.ac.jp
D001665:Binding Sites; D005192:Family Health; D005337:Fibrin / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D005340:Fibrinogen / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D015241:Fibrinogens, Abnormal / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D006801:Humans; D013329:Structure-Activity Relationship
D015241:Fibrinogens, Abnormal; D005337:Fibrin; D005340:Fibrinogen