Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor.

Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor. Research Abstract Details 

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Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor. Abstract Text:

M Odaka,D Kohda,I Lax,J Schlessinger,F Inagaki,

We studied the dimerization of the recombinant soluble extracellular domain of the epidermal growth factor receptor (sEGFR) in response to EGF-binding using multi-angle laser light scattering with size exclusion chromatography (SEC-MALLS). In the absence of EGF, sEGFR behaved as a monomer. However, upon EGF-binding, sEGFR formed a dimer with the stoichiometry of two EGF molecules bound to two sEGFR molecules [(EGF)2-(sEGFR)2]. We analyzed the chemical equilibrium of the dimer formation by SEC-MALLS using a dissociation constant of 0.25 microM for the binding of EGF to sEGFR. The calculated dissociation constant for EGF-induced sEGFR dimerization was found to be 2.4 +/- 0.9 microM. These experiments demonstrated that EGF induces receptor dimerization and that two EGF molecules are bound to an EGF-receptor dimer.

Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor. Publishing Authors By Initials

M Odaka,D Kohda,I Lax,J Schlessinger,F Inagaki,

For similar natural sciences: chemistry: chemistry, physical: solubility research abstracts see: natural sciences: chemistry: chemistry, physical: solubility research

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Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 122

Page Numbers: 116-21

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 1997

Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor. Keywords Mesh Terms:

KEYWORDS: Solubility

MESH TERMS: metabolism

Chemical & Substance for Abstract: Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor. Information

Substance Name: Receptor, Epidermal Growth Factor

Registry Number: EC 2.7.1.112

Grant and Affiliation Information for Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor.

AFFILIATION: Department of Molecular Physiology, The Tokyo Metropolitan Institute of Medical Science, Japan.

Country: JAPAN

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MEDLINETA: J Biochem

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