Literature DB >> 8578468

Conformational changes in adhesive proteins modulate their adhesive function.

T Ugarova1, F R Agbanyo, E F Plow.   

Abstract

A large family of glycoproteins mediates cell adhesion by binding to cellular receptors. As a group, these adhesive proteins are large in size, multi-domainal in composition, and are capable of self-association. A general property of the adhesive proteins is their susceptibility to structural modulation, and conformational change provides a mechanism for regulation of their adhesive functions. To illustrate this concept, conformational alterations of thrombospondin, fibrinogen and fibronectin are shown to modulate their adhesive potential. Thus, conformational status of the adhesive proteins contributes to the regulation of cell adhesion.

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Year:  1995        PMID: 8578468

Source DB:  PubMed          Journal:  Thromb Haemost        ISSN: 0340-6245            Impact factor:   5.249


  3 in total

1.  Bivalent ligation of the collagen-binding modules of fibronectin by SFS, a non-anchored bacterial protein of Streptococcus equi.

Authors:  Wenjiang Ma; Hanqing Ma; Frances J Fogerty; Deane F Mosher
Journal:  J Biol Chem       Date:  2014-12-18       Impact factor: 5.157

2.  Phosphatidylserine-positive erythrocytes bind to immobilized and soluble thrombospondin-1 via its heparin-binding domain.

Authors:  Suhita Gayen Betal; B N Yamaja Setty
Journal:  Transl Res       Date:  2008-09-04       Impact factor: 7.012

3.  Borrelia burgdorferi protein BBK32 binds to soluble fibronectin via the N-terminal 70-kDa region, causing fibronectin to undergo conformational extension.

Authors:  Gemma Harris; Wenjiang Ma; Lisa M Maurer; Jennifer R Potts; Deane F Mosher
Journal:  J Biol Chem       Date:  2014-06-24       Impact factor: 5.157

  3 in total

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