The conformational switch in muscarinic acetylcholine receptors

E. C. Hulme; Z. L. Lu; M. Bee; C. A.M. Curtis; J. Saldanha

doi:10.1016/S0024-3205(01)01044-X

The conformational switch in muscarinic acetylcholine receptors

E. C. Hulme^*, Z. L. Lu, M. Bee, C. A.M. Curtis, J. Saldanha

^*Corresponding author for this work

Medical Research Council

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

25 Citations (Scopus)

Abstract

The recently-determined structure of rhodopsin has provided a suitable basis for modeling the three-dimensional structure of the M ₁ muscarinic acetylcholine receptor. Using this as a framework for interpreting mutagenesis studies, we have been able to suggest most of the contacts which the receptor makes with acetylcholine and many of the intramolecular contacts which are important for the ground-state structure of the receptor. It is possible to outline a mechanism of G-protein interaction.

Original language	English
Pages (from-to)	2495-2500
Number of pages	6
Journal	Life Sciences
Volume	68
Issue number	22-23
DOIs	https://doi.org/10.1016/S0024-3205(01)01044-X
Publication status	Published - 27 Apr 2001
Externally published	Yes

Keywords

Acetylcholine
G-protein
Muscarinic
Rhodopsin

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10.1016/S0024-3205(01)01044-X

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AU - Hulme, E. C.

AU - Lu, Z. L.

AU - Bee, M.

AU - Curtis, C. A.M.

AU - Saldanha, J.

PY - 2001/4/27

Y1 - 2001/4/27

N2 - The recently-determined structure of rhodopsin has provided a suitable basis for modeling the three-dimensional structure of the M 1 muscarinic acetylcholine receptor. Using this as a framework for interpreting mutagenesis studies, we have been able to suggest most of the contacts which the receptor makes with acetylcholine and many of the intramolecular contacts which are important for the ground-state structure of the receptor. It is possible to outline a mechanism of G-protein interaction.

AB - The recently-determined structure of rhodopsin has provided a suitable basis for modeling the three-dimensional structure of the M 1 muscarinic acetylcholine receptor. Using this as a framework for interpreting mutagenesis studies, we have been able to suggest most of the contacts which the receptor makes with acetylcholine and many of the intramolecular contacts which are important for the ground-state structure of the receptor. It is possible to outline a mechanism of G-protein interaction.

KW - Acetylcholine

KW - G-protein

KW - Muscarinic

KW - Rhodopsin

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U2 - 10.1016/S0024-3205(01)01044-X

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JO - Life Sciences

JF - Life Sciences

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ER -

The conformational switch in muscarinic acetylcholine receptors

Abstract

Keywords

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