Scanning mutagenesis of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor

Edward C. Hulme; Zhi Liang Lu

doi:10.1016/S0928-4257(98)80031-4

Scanning mutagenesis of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor

Edward C. Hulme^*
, Zhi Liang Lu

^*Corresponding author for this work

Medical Research Council

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

13 Citations (Scopus)

Abstract

Scanning mutagenesis of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor has revealed a highly-differentiated α-helical structure. Lipid-facing residues are distinguished from a patch of residues which selectively stabilise the ground state of the receptor, and from a band of amino acids extending the full length of the helix, which contribute to the active agonist-receptor-G protein complex. The most important residues are strongly conserved in the GPCR superfamily.

Original language	English
Pages (from-to)	269-274
Number of pages	6
Journal	Journal of Physiology Paris
Volume	92
Issue number	3-4
DOIs	https://doi.org/10.1016/S0928-4257(98)80031-4
Publication status	Published - 1998
Externally published	Yes

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10.1016/S0928-4257(98)80031-4

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title = "Scanning mutagenesis of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor",

abstract = "Scanning mutagenesis of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor has revealed a highly-differentiated α-helical structure. Lipid-facing residues are distinguished from a patch of residues which selectively stabilise the ground state of the receptor, and from a band of amino acids extending the full length of the helix, which contribute to the active agonist-receptor-G protein complex. The most important residues are strongly conserved in the GPCR superfamily.",

author = "Hulme, \{Edward C.\} and Lu, \{Zhi Liang\}",

note = "Funding Information: This work was supported by the Medical Research Council (U.K.) and by the Wellcome Trust.",

year = "1998",

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T1 - Scanning mutagenesis of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor

AU - Hulme, Edward C.

AU - Lu, Zhi Liang

N1 - Funding Information: This work was supported by the Medical Research Council (U.K.) and by the Wellcome Trust.

PY - 1998

Y1 - 1998

N2 - Scanning mutagenesis of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor has revealed a highly-differentiated α-helical structure. Lipid-facing residues are distinguished from a patch of residues which selectively stabilise the ground state of the receptor, and from a band of amino acids extending the full length of the helix, which contribute to the active agonist-receptor-G protein complex. The most important residues are strongly conserved in the GPCR superfamily.

AB - Scanning mutagenesis of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor has revealed a highly-differentiated α-helical structure. Lipid-facing residues are distinguished from a patch of residues which selectively stabilise the ground state of the receptor, and from a band of amino acids extending the full length of the helix, which contribute to the active agonist-receptor-G protein complex. The most important residues are strongly conserved in the GPCR superfamily.

UR - https://www.scopus.com/pages/publications/0032105388

U2 - 10.1016/S0928-4257(98)80031-4

DO - 10.1016/S0928-4257(98)80031-4

M3 - Article

C2 - 9789821

AN - SCOPUS:0032105388

SN - 0928-4257

VL - 92

SP - 269

EP - 274

JO - Journal of Physiology Paris

JF - Journal of Physiology Paris

IS - 3-4

ER -

Scanning mutagenesis of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor

Abstract

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