title: Structure-function relationships in factor IX and factor IXa.
abstract: Factor IX (FIX) consists of an N-terminal gamma-carboxyglutamic acid (Gla) domain followed by two epidermal growth factor (EGF)-like domains, and the C-terminal serine protease domain. During physiologic coagulation, one of the activators of FIX is the FVIIa/tissue factor (TF) complex. In this reaction, the Gla and EGF1 domains of FIX are thought to interact with TF. The FIXa that is generated then combines with FVIIIa on the platelet surface to activate FX in the coagulation cascade. In this assembly, the protease domain and possibly the EGF2 domain of FIXa are thought to provide the primary specificity in binding to FVIIIa. Disruption of the interaction of FIX/FX with TF and of the FIXa:FVIIIa interface may provide a pharmacologic target as an alternative strategy for the development of antithrombotic agents.
authors.affiliation: Departments of Pharmacological & Physiological Sciences and Internal Medicine, Saint Louis University Health Sciences Center, MO 63110, USA.
authors.forename: Amy E
authors.initials: AE
authors.lastname: Schmidt
authors.forename: S Paul
authors.initials: SP
authors.lastname: Bajaj
mesh_terms: D001777:Blood Coagulation / Q000187:drug effects; D005164:Factor IX / Q000737:chemistry* / Q000494:pharmacology*; D015949:Factor IXa / Q000737:chemistry* / Q000494:pharmacology*; D006801:Humans; D015398:Signal Transduction / Q000187:drug effects; D013329:Structure-Activity Relationship
chemical_list: D005164:Factor IX; D015949:Factor IXa