Ontology highlight
ABSTRACT:
SUBMITTER: Sakkal LA
PROVIDER: S-EPMC5403616 | biostudies-literature | 2017 Jun
REPOSITORIES: biostudies-literature
Journal of computational chemistry 20170128 15
Following insights from recent crystal structures of the muscarinic acetylcholine receptor, binding modes of Positive Allosteric Modulators (PAMs) were predicted under the assumption that PAMs should bind to the extracellular surface of the active state. A series of well-characterized PAMs for adenosine (A<sub>1</sub> R, A<sub>2A</sub> R, A<sub>3</sub> R) and muscarinic acetylcholine (M<sub>1</sub> R, M<sub>5</sub> R) receptors were modeled using both rigid and flexible receptor CHARMM-based mol ...[more]