TY - JOUR
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 - http://www.scopus.com/inward/record.url?scp=0032105388&partnerID=8YFLogxK
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 -