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Structural and functional role of the beta-strand insert (gamma 381-390) in the fibrinogen gamma-module. A "pull out"
S Yakovlev1, D Loukinov, L Medved
1Biochemistry Department, Holland Laboratory, American Red Cross, 15601 Crabbs Branch Way, Rockville, MD 20855, USA. yakovles@usa.redcross.org
Annals of the New York Academy of Sciences
|July 20, 2001
Abstract:
Study of the folding status of the fibrinogen gamma-module (residues gamma 148-411) revealed that its COOH-terminal beta-strand (residues gamma 381-390), that is normally inserted into its central domain, can be removed without destroying its compact structure. Based on this and other observations we propose a "pull out" hypothesis that suggests a mechanism for the formation of transverse gamma-gamma crosslinks in fibrin.