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The secreted form of the epidermal growth factor receptor. Characterization and crystallization of the receptor-ligand complex.

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The secreted form of the epidermal growth factor receptor. Characterization and crystallization of the receptor-ligand complex. / Günther, N; Betzel, C; Weber, Wolfgang.

In: J BIOL CHEM, Vol. 265, No. 36, 36, 1990, p. 22082-22085.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Günther, N, Betzel, C & Weber, W 1990, 'The secreted form of the epidermal growth factor receptor. Characterization and crystallization of the receptor-ligand complex.', J BIOL CHEM, vol. 265, no. 36, 36, pp. 22082-22085. <http://www.ncbi.nlm.nih.gov/pubmed/2266111?dopt=Citation>

APA

Günther, N., Betzel, C., & Weber, W. (1990). The secreted form of the epidermal growth factor receptor. Characterization and crystallization of the receptor-ligand complex. J BIOL CHEM, 265(36), 22082-22085. [36]. http://www.ncbi.nlm.nih.gov/pubmed/2266111?dopt=Citation

Vancouver

Günther N, Betzel C, Weber W. The secreted form of the epidermal growth factor receptor. Characterization and crystallization of the receptor-ligand complex. J BIOL CHEM. 1990;265(36):22082-22085. 36.

Bibtex

@article{a85e70b01aeb47508ca5b79036fc89bd,
title = "The secreted form of the epidermal growth factor receptor. Characterization and crystallization of the receptor-ligand complex.",
abstract = "A protein composed of the external domain of the epidermal growth factor (EGF) receptor is secreted by A431 human tumor cells. The soluble receptor protein was isolated in bulk quantities from cell culture supernatants. It has an intact ligand binding site, exists in a 93-kDa monomeric form, and does not undergo oligomerization upon ligand binding; thus the receptor dimerization reported for the EGF holoreceptor appears not to be a function of its external domain. The unique system of a physiological soluble receptor was utilized for a crystallization study. Crystals were obtained but only in the presence of the ligand. They contained (in equimolar amounts) receptor as well as EGF. The crystals belong to the tetragonal space group P4(3)2(1)2 or P4(1)2(1)2 with unit cell dimensions a = b = 118 A, c = 202 A. The packing density parameter was 3.55 A3/dalton, indicating the asymmetric unit to consist of one receptor-ligand complex.",
keywords = "Humans, Ligands, Kinetics, Immunoblotting, Cell Line, Centrifugation, Density Gradient, Molecular Weight, X-Ray Diffraction, Crystallization, Epidermal Growth Factor/isolation & purification/*metabolism, Humans, Ligands, Kinetics, Immunoblotting, Cell Line, Centrifugation, Density Gradient, Molecular Weight, X-Ray Diffraction, Crystallization, Epidermal Growth Factor/isolation & purification/*metabolism",
author = "N G{\"u}nther and C Betzel and Wolfgang Weber",
year = "1990",
language = "English",
volume = "265",
pages = "22082--22085",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "36",

}

RIS

TY - JOUR

T1 - The secreted form of the epidermal growth factor receptor. Characterization and crystallization of the receptor-ligand complex.

AU - Günther, N

AU - Betzel, C

AU - Weber, Wolfgang

PY - 1990

Y1 - 1990

N2 - A protein composed of the external domain of the epidermal growth factor (EGF) receptor is secreted by A431 human tumor cells. The soluble receptor protein was isolated in bulk quantities from cell culture supernatants. It has an intact ligand binding site, exists in a 93-kDa monomeric form, and does not undergo oligomerization upon ligand binding; thus the receptor dimerization reported for the EGF holoreceptor appears not to be a function of its external domain. The unique system of a physiological soluble receptor was utilized for a crystallization study. Crystals were obtained but only in the presence of the ligand. They contained (in equimolar amounts) receptor as well as EGF. The crystals belong to the tetragonal space group P4(3)2(1)2 or P4(1)2(1)2 with unit cell dimensions a = b = 118 A, c = 202 A. The packing density parameter was 3.55 A3/dalton, indicating the asymmetric unit to consist of one receptor-ligand complex.

AB - A protein composed of the external domain of the epidermal growth factor (EGF) receptor is secreted by A431 human tumor cells. The soluble receptor protein was isolated in bulk quantities from cell culture supernatants. It has an intact ligand binding site, exists in a 93-kDa monomeric form, and does not undergo oligomerization upon ligand binding; thus the receptor dimerization reported for the EGF holoreceptor appears not to be a function of its external domain. The unique system of a physiological soluble receptor was utilized for a crystallization study. Crystals were obtained but only in the presence of the ligand. They contained (in equimolar amounts) receptor as well as EGF. The crystals belong to the tetragonal space group P4(3)2(1)2 or P4(1)2(1)2 with unit cell dimensions a = b = 118 A, c = 202 A. The packing density parameter was 3.55 A3/dalton, indicating the asymmetric unit to consist of one receptor-ligand complex.

KW - Humans

KW - Ligands

KW - Kinetics

KW - Immunoblotting

KW - Cell Line

KW - Centrifugation, Density Gradient

KW - Molecular Weight

KW - X-Ray Diffraction

KW - Crystallization

KW - Epidermal Growth Factor/isolation & purification/metabolism

KW - Humans

KW - Ligands

KW - Kinetics

KW - Immunoblotting

KW - Cell Line

KW - Centrifugation, Density Gradient

KW - Molecular Weight

KW - X-Ray Diffraction

KW - Crystallization

KW - Epidermal Growth Factor/isolation & purification/metabolism

M3 - SCORING: Journal article

VL - 265

SP - 22082

EP - 22085

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 36

M1 - 36

ER -