Structure and function of an acetylcholine receptor

J. Kistler; R. M. Stroud; M. W. Klymkowsky; R. A. Lalancette; R. H. Fairclough

doi:10.1016/S0006-3495(82)84685-7

Structure and function of an acetylcholine receptor

J. Kistler, R. M. Stroud, M. W. Klymkowsky, R. A. Lalancette, R. H. Fairclough

Research output: Contribution to journal › Article › peer-review

166 Scopus citations

Abstract

Structural analysis of an acetylcholine receptor from Torpedo californica leads to a three-dimensional model in which a "monomeric" receptor is shown to contain subunits arranged around a central ionophoretic channel, which in turn traverses the entire 110 A length of the molecule. The receptor extends approximately 15 A on the cytoplasmic side, 55 A on the synaptic side of the membrane. The alpha-bungarotoxin/agonist binding site is found to be approximately 55 A from the entrance to the central gated ion channel. A hypothesis for the mechanism of AcChR is presented which takes into account the structural and kinetic data, which is testable, and which serves as a focus for future studies on the agonist-induced structure change in AcChR.

Original language	English (US)
Pages (from-to)	371-383
Number of pages	13
Journal	Biophysical Journal
Volume	37
Issue number	1
DOIs	https://doi.org/10.1016/S0006-3495(82)84685-7
State	Published - 1982
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics

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10.1016/S0006-3495(82)84685-7

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title = "Structure and function of an acetylcholine receptor",

abstract = "Structural analysis of an acetylcholine receptor from Torpedo californica leads to a three-dimensional model in which a {"}monomeric{"} receptor is shown to contain subunits arranged around a central ionophoretic channel, which in turn traverses the entire 110 A length of the molecule. The receptor extends approximately 15 A on the cytoplasmic side, 55 A on the synaptic side of the membrane. The alpha-bungarotoxin/agonist binding site is found to be approximately 55 A from the entrance to the central gated ion channel. A hypothesis for the mechanism of AcChR is presented which takes into account the structural and kinetic data, which is testable, and which serves as a focus for future studies on the agonist-induced structure change in AcChR.",

author = "J. Kistler and Stroud, {R. M.} and Klymkowsky, {M. W.} and Lalancette, {R. A.} and Fairclough, {R. H.}",

note = "Funding Information: This work was supported by grant PCM80-21433 from the United States National Science Foundation to Dr. Stroud, by grants GM24485 and GM25217 from the National Institutes of Health to Dr. Stroud, by a Swiss National Science Foundation postdoctoral fellowship to Dr. Kistl- er, and by a National Cancer Institute postdoctoral fellowship to Dr. Fairclough. Receivedfor publication 20 April 1981.",

year = "1982",

doi = "10.1016/S0006-3495(82)84685-7",

language = "English (US)",

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T1 - Structure and function of an acetylcholine receptor

AU - Kistler, J.

AU - Stroud, R. M.

AU - Klymkowsky, M. W.

AU - Lalancette, R. A.

AU - Fairclough, R. H.

N1 - Funding Information: This work was supported by grant PCM80-21433 from the United States National Science Foundation to Dr. Stroud, by grants GM24485 and GM25217 from the National Institutes of Health to Dr. Stroud, by a Swiss National Science Foundation postdoctoral fellowship to Dr. Kistl- er, and by a National Cancer Institute postdoctoral fellowship to Dr. Fairclough. Receivedfor publication 20 April 1981.

PY - 1982

Y1 - 1982

N2 - Structural analysis of an acetylcholine receptor from Torpedo californica leads to a three-dimensional model in which a "monomeric" receptor is shown to contain subunits arranged around a central ionophoretic channel, which in turn traverses the entire 110 A length of the molecule. The receptor extends approximately 15 A on the cytoplasmic side, 55 A on the synaptic side of the membrane. The alpha-bungarotoxin/agonist binding site is found to be approximately 55 A from the entrance to the central gated ion channel. A hypothesis for the mechanism of AcChR is presented which takes into account the structural and kinetic data, which is testable, and which serves as a focus for future studies on the agonist-induced structure change in AcChR.

AB - Structural analysis of an acetylcholine receptor from Torpedo californica leads to a three-dimensional model in which a "monomeric" receptor is shown to contain subunits arranged around a central ionophoretic channel, which in turn traverses the entire 110 A length of the molecule. The receptor extends approximately 15 A on the cytoplasmic side, 55 A on the synaptic side of the membrane. The alpha-bungarotoxin/agonist binding site is found to be approximately 55 A from the entrance to the central gated ion channel. A hypothesis for the mechanism of AcChR is presented which takes into account the structural and kinetic data, which is testable, and which serves as a focus for future studies on the agonist-induced structure change in AcChR.

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Structure and function of an acetylcholine receptor

Abstract

All Science Journal Classification (ASJC) codes

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