(Q52209541)

27 April 2018

title

A dimeric ternary complex of FGFR [correction of FGFR1], heparin and FGF-1 leads to an 'electrostatic sandwich' model for heparin binding. (English)

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27 April 2018

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2

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27 April 2018

author name string

M T Huhtala

series ordinal

1

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27 April 2018

M S Johnson

series ordinal

3

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27 April 2018

publication date

1 June 1999

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27 April 2018

published in

Structure

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27 April 2018

volume

7

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27 April 2018

issue

6

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27 April 2018

page(s)

699-709

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27 April 2018

An essential heparin-binding domain in the fibroblast growth factor receptor kinase

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Heparin-induced oligomerization of FGF molecules is responsible for FGF receptor dimerization, activation, and cell proliferation

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Molecular cloning and characterization of a second subunit of the interleukin 1 receptor complex

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The IL1 receptor accessory protein is responsible for the recruitment of the interleukin-1 receptor associated kinase to the IL1/IL1 receptor I complex

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Crystal structure of the type-I interleukin-1 receptor complexed with interleukin-1beta

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A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist

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Structure of a heparin-linked biologically active dimer of fibroblast growth factor

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The role of heparin in the complex formation between fibroblast growth factor 2 and its high affinity receptor: comparative modelling and biochemical studies

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Many of the immunoglobulin superfamily domains in cell adhesion molecules and surface receptors belong to a new structural set which is close to that containing variable domains

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Outline structures for the extracellular domains of the fibroblast growth factor receptors

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X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 A resolution

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Copper and calcium binding motifs in the extracellular domains of fibroblast growth factor receptors

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7 January 2021

Heparin structure and interactions with basic fibroblast growth factor

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Glu-96 of basic fibroblast growth factor is essential for high affinity receptor binding. Identification by structure-based site-directed mutagenesis

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Molecular modeling and deletion mutagenesis implicate the nuclear translocation sequence in structural integrity of fibroblast growth factor-1.

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7 January 2021

Multivalent Ligand-Receptor Binding Interactions in the Fibroblast Growth Factor System Produce a Cooperative Growth Factor and Heparin Mechanism for Receptor Dimerization

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Human growth hormone and extracellular domain of its receptor: crystal structure of the complex

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Preferential self-association of basic fibroblast growth factor is stabilized by heparin during receptor dimerization and activation.

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7 January 2021

Heparin-induced self-association of fibroblast growth factor-2. Evidence for two oligomerization processes

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Properly oriented heparin-decasaccharide-induced dimers are the biologically active form of basic fibroblast growth factor.

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Molecular modeling based mutagenesis defines ligand binding and specificity determining regions of fibroblast growth factor receptors

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A homeo-interaction sequence in the ectodomain of the fibroblast growth factor receptor

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7 January 2021

Divalent cations and heparin/heparan sulfate cooperate to control assembly and activity of the fibroblast growth factor receptor complex

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7 January 2021

New insights into heparin-induced FGF oligomerization

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7 January 2021

A Structural Basis for Sequence Comparisons

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Discrimination of common protein folds: application of protein structure to sequence/structure comparisons

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Identifiers

DOI

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27 April 2018

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27 April 2018