title: [Thrombin: structure-function relationship in biochemical interactions].
abstract: Data on the content and localization of the recognition site (exosite) for high molecular weight substrates in the thrombin molecule have been summarized. It has been shown that this center, which binds anion sites of macromolecules, plays a key role in regulation of thrombin activity. Data of a proteolytic mechanism of platelet receptor activation by thrombin are reported. Prospects in biomedical studies of thrombin derivatives are discussed with the emphasis on developing new therapeutic tools and combined courses of thrombolytic therapy. Possibilities are discussed of developing a computer model of thrombin interactions for theoretical and applied purposes.
authors.forename: A V
authors.initials: AV
authors.lastname: Maksimenko
mesh_terms: D001665:Binding Sites; D001792:Blood Platelets / Q000187:drug effects; D003198:Computer Simulation; D006868:Hydrolysis; D013329:Structure-Activity Relationship; D013917:Thrombin / Q000737:chemistry / Q000378:metabolism* / Q000494:pharmacology
chemical_list: D013917:Thrombin
vernacular_title: Trombin: sootnoshenie struktura-funktsiia v biokhimicheskikh vzaimodeĭstviiakh.