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    Cooperative heparin-mediated oligomerization of fibroblast growth factor-1 (FGF1) precedes recruitment of FGFR2 to ternary complexes.

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    Authors
    Brown, A
    Robinson, Christopher J
    Gallagher, John T
    Blundell, T
    Affiliation
    Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom. ab604@cam.ac.uk
    Issue Date
    2013-04-16
    
    Metadata
    Show full item record
    Abstract
    Fibroblast growth factors (FGFs) utilize cell surface heparan sulfate as a coreceptor in the assembly of signaling complexes with FGF-receptors on the plasma membrane. Here we undertake a complete thermodynamic characterization of the assembly of the FGF signaling complex using isothermal titration calorimetry. Heparin fragments of defined length are used as chemical analogs of the sulfated domains of heparan sulfate and examined for their ability to oligomerize FGF1. Binding is modeled using the McGhee-von Hippel formalism for the cooperative binding of ligands to a monodimensional lattice. Oligomerization of FGFs on heparin is shown to be mediated by positive cooperativity (α = 6). Heparin octasaccharide is the shortest length capable of dimerizing FGF1 and on longer heparin chains FGF1 binds with a minimal footprint of 4.2 saccharide units. The thermodynamics and stoichiometry of the ternary complex suggest that in solution FGF1 binds to heparin in a trans-dimeric manner before FGFR recruitment.
    Citation
    Cooperative heparin-mediated oligomerization of fibroblast growth factor-1 (FGF1) precedes recruitment of FGFR2 to ternary complexes. 2013, 104 (8):1720-30 Biophys J
    Journal
    Biophysical Journal
    URI
    http://hdl.handle.net/10541/294892
    DOI
    10.1016/j.bpj.2013.02.051
    PubMed ID
    23601319
    Type
    Article
    Language
    en
    ISSN
    1542-0086
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.bpj.2013.02.051
    Scopus Count
    Collections
    All Paterson Institute for Cancer Research

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