title: Structural and functional role of the beta-strand insert (gamma 381-390) in the fibrinogen gamma-module. A "pull out" hypothesis.
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.
authors.affiliation: Biochemistry Department, Holland Laboratory, American Red Cross, 15601 Crabbs Branch Way, Rockville, MD 20855, USA. yakovles@usa.redcross.org
authors.forename: S
authors.initials: S
authors.lastname: Yakovlev
authors.forename: D
authors.initials: D
authors.lastname: Loukinov
authors.forename: L
authors.initials: L
authors.lastname: Medved
mesh_terms: D005340:Fibrinogen / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D011487:Protein Conformation; D013329:Structure-Activity Relationship
chemical_list: D005340:Fibrinogen