Literature DB >> 11460468

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

S Yakovlev1, D Loukinov, L Medved.   

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.

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Year:  2001        PMID: 11460468

Source DB:  PubMed          Journal:  Ann N Y Acad Sci        ISSN: 0077-8923            Impact factor:   5.691


  2 in total

1.  Mechanism of fibrin(ogen) forced unfolding.

Authors:  Artem Zhmurov; Andre E X Brown; Rustem I Litvinov; Ruxandra I Dima; John W Weisel; Valeri Barsegov
Journal:  Structure       Date:  2011-11-09       Impact factor: 5.006

2.  Mechanical transition from α-helical coiled coils to β-sheets in fibrin(ogen).

Authors:  Artem Zhmurov; Olga Kononova; Rustem I Litvinov; Ruxandra I Dima; Valeri Barsegov; John W Weisel
Journal:  J Am Chem Soc       Date:  2012-09-25       Impact factor: 15.419

  2 in total

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