Structure and selectivity engineering of the M 1 muscarinic receptor toxin complex | Zendy

Shoji Maeda | Zendy; Jun Xu | Zendy; Francois Marie Ngako Kadji | Zendy; Mary J. Clark | Zendy; Jiawei Zhao | Zendy; Naotaka Tsutsumi | Zendy; Junken Aoki | Zendy; Roger K. Sunahara | Zendy; Asuka Inoue | Zendy; K. Christopher García | Zendy; Brian K. Kobilka | Zendy

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Structure and selectivity engineering of the M ₁ muscarinic receptor toxin complex

Author(s) -

Shoji Maeda,

Jun Xu,

Francois Marie Ngako Kadji,

Mary J. Clark,

Jiawei Zhao,

Naotaka Tsutsumi,

Junken Aoki,

Roger K. Sunahara,

Asuka Inoue,

K. Christopher García,

Brian K. Kobilka

Publication year - 2020

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aax2517

Subject(s) - muscarinic acetylcholine receptor , toxin , selectivity , chemistry , receptor , biochemistry , catalysis

Engineering a toxin Developing drugs that target a specific subtype in a G protein–coupled receptor (GPCR) family is a major challenge. Maedaet al. examined the basis of specificity of a snake venom toxin binding to muscarinic acetylcholine receptors (MAChRs), which mediate many functions of the central and parasympathetic nervous systems. They determined a structure that shows why the mamba venom toxin MT7 is specific for one receptor, M1 AChR, and also explains how it inhibits downstream signaling. Based on this structure, they engineered MT7 to be selective for another receptor, M2 AChR, instead of M1 ChR. The toxin may present a promising scaffold for developing specific GPCR modulators.Science , this issue p.161

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