Structure-based discovery of selective positive allosteric modulators of antagonists for the M2 muscarinic acetylcholine receptor

Proceedings of the National Academy of Sciences of the United States of America

Volumn 115, Issue 10, 2018, Pages E2419-E2428

  Korczynska, Magdalena ^a   Clark, Mary J ^b   Valant, Celine ^c   Xu, Jun ^d   Moo, Ee Von ^c   Albold, Sabine ^c   Weiss, Dahlia R ^a   Torosyan, Hayarpi ^a   Huang, Weijiao ^e   Kruse, Andrew C ^f   Lyda, Brent R ^b   May, Lauren T ^c   Baltos, Jo Anne ^c   Sexton, Patrick M ^c   Kobilka, Brian K ^d,e   Christopoulos, Arthur ^c   Shoichet, Brian K ^a   Sunahara, Roger K ^b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c MONASH UNIVERSITY   (Australia)

^d Tsinghua University   (China)

^e STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^f HARVARD MEDICAL SCHOOL   (United States)

Author keywords

Docking; GPCR; PAM antagonist; Structure based ligand discovery; Subtype selectivity

Indexed keywords

METHYLSCOPOLAMINE; MITOGEN ACTIVATED PROTEIN KINASE 1; MUSCARINIC M2 RECEPTOR; MUSCARINIC M2 RECEPTOR ANTAGONIST; LIGAND; MITOGEN ACTIVATED PROTEIN KINASE 3; MUSCARINIC AGENT; PROTEIN BINDING;

ADULT; ALLOSTERISM; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; BINDING SITE; CARDIAC MUSCLE CELL; CONTROLLED STUDY; HYPOTHALAMUS; LIGAND BINDING; MOLECULAR DOCKING; MOLECULAR PROBE; NEWBORN; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROCESS OPTIMIZATION; PROTEIN PHOSPHORYLATION; RAT; STRUCTURE ACTIVITY RELATION; ALLOSTERIC SITE; ANIMAL; CHEMISTRY; HUMAN; KINETICS; METABOLISM; PHOSPHORYLATION;

ALLOSTERIC REGULATION; ALLOSTERIC SITE; ANIMALS; HUMANS; KINETICS; LIGANDS; MITOGEN-ACTIVATED PROTEIN KINASE 1; MITOGEN-ACTIVATED PROTEIN KINASE 3; MOLECULAR DOCKING SIMULATION; MUSCARINIC AGONISTS; PHOSPHORYLATION; PROTEIN BINDING; RATS; RECEPTOR, MUSCARINIC M2;

EID: 85042923595     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1718037115     Document Type: Article

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