Conformational changes in adhesive proteins modulate their adhesive function

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 modula...

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Bibliographic Details
Published inThrombosis and haemostasis Vol. 74; no. 1; p. 253
Main Authors Ugarova, T, Agbanyo, F R, Plow, E F
Format Journal Article
LanguageEnglish
Published Germany 01.07.1995
Subjects
Cell Adhesion
Cell Adhesion Molecules - chemistry
Cell Adhesion Molecules - physiology
Fibrinogen - chemistry
Fibrinogen - physiology
Fibronectins - chemistry
Fibronectins - physiology
Humans
Membrane Glycoproteins - chemistry
Membrane Glycoproteins - physiology
Protein Conformation
Thrombospondins
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Summary: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.
ISSN:0340-6245
DOI:10.1055/s-0038-1642686