Structural insights into the subtype-selective antagonist binding to the M2 muscarinic receptor View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2018-12

AUTHORS

Ryoji Suno, Sangbae Lee, Shoji Maeda, Satoshi Yasuda, Keitaro Yamashita, Kunio Hirata, Shoichiro Horita, Maki S. Tawaramoto, Hirokazu Tsujimoto, Takeshi Murata, Masahiro Kinoshita, Masaki Yamamoto, Brian K. Kobilka, Nagarajan Vaidehi, So Iwata, Takuya Kobayashi

ABSTRACT

Human muscarinic receptor M2 is one of the five subtypes of muscarinic receptors belonging to the family of G-protein-coupled receptors. Muscarinic receptors are targets for multiple neurodegenerative diseases. The challenge has been designing subtype-selective ligands against one of the five muscarinic receptors. We report high-resolution structures of a thermostabilized mutant M2 receptor bound to a subtype-selective antagonist AF-DX 384 and a nonselective antagonist NMS. The thermostabilizing mutation S110R in M2 was predicted using a theoretical strategy previously developed in our group. Comparison of the crystal structures and pharmacological properties of the M2 receptor shows that the Arg in the S110R mutant mimics the stabilizing role of the sodium cation, which is known to allosterically stabilize inactive state(s) of class A GPCRs. Molecular dynamics simulations reveal that tightening of the ligand-residue contacts in M2 receptors compared to M3 receptors leads to subtype selectivity of AF-DX 384. More... »

PAGES

1150-1158

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41589-018-0152-y

DOI

http://dx.doi.org/10.1038/s41589-018-0152-y

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1108043124

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30420692


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