Diversity Does Make a Difference: Fibroblast Growth Factor - HeparinInteractions

Loading...
Thumbnail Image

ORCID

https://orcid.org/0000-0003-2219-5833

Other Contributors

Issue Date

Type

Article

Language

ENG

Degree

Research Projects

Organizational Units

Journal Issue

Alternative Title

Abstract

Fibroblast growth factors (FGFs) are members of a protein family with a broad range of biological activities. The best characterized FGFs interact with two distinct extracellular receptors — a transmembrane tyrosine kinase FGF receptor (FGFR) and a heparan sulfate-related proteoglycan of the extracellular matrix. These components form a FGF—FGFR—proteoglycan complex that activates the FGF-mediated signal transduction process through FGFR dimerization. Recent crystal structure determinations of FGF—heparin complexes have provided insights into both the interactions between these components and the role of heparin-like proteoglycans in FGF function. Future advances in this field will benefit enormously from an ability to specifically prepare homogenous heparin-based oligosaccharides of defined sequence for use in biochemical and structural studies of FGF and many other systems.

Description

Current Opinions in Structural Biology, 8, 578-586
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.

Full Citation

Diversity Does Make a Difference: Fibroblast Growth Factor - HeparinInteractions, S. Faham, R.J. Linhardt, D.C. Rees, Current Opinionsin Structural Biology, 8, 578-586 1998.

Publisher

Terms of Use

Journal

Volume

Issue

PubMed ID

DOI

ISSN

EISSN

Endorsement

Review

Supplemented By

Referenced By