Structural and functional role of the beta-strand insert (gamma 381-390) in the fibrinogen gamma-module. A "pull out" hypothesis

Structural and functional role of the beta-strand insert (gamma 381-390) in the fibrinogen gamma-module. A "pull out" hypothesis

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 w...

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Veröffentlicht in:Annals of the New York Academy of Sciences 2001-01, Vol.936 (1), p.122-124
Hauptverfasser: Yakovlev, S, Loukinov, D, Medved, L
Format: Artikel
Sprache:eng
Schlagworte:
Fibrinogen - chemistry
Fibrinogen - metabolism
Humans
Protein Conformation
Structure-Activity Relationship
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Zusammenfassung: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.
ISSN:0077-8923
1749-6632
DOI:10.1111/j.1749-6632.2001.tb03499.x