Activation and allosteric modulation of a muscarinic acetylcholine receptor View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2013-12

AUTHORS

Andrew C. Kruse, Aaron M. Ring, Aashish Manglik, Jianxin Hu, Kelly Hu, Katrin Eitel, Harald Hübner, Els Pardon, Celine Valant, Patrick M. Sexton, Arthur Christopoulos, Christian C. Felder, Peter Gmeiner, Jan Steyaert, William I. Weis, K. Christopher Garcia, Jürgen Wess, Brian K. Kobilka

ABSTRACT

Despite recent advances in crystallography and the availability of G-protein-coupled receptor (GPCR) structures, little is known about the mechanism of their activation process, as only the β2 adrenergic receptor (β2AR) and rhodopsin have been crystallized in fully active conformations. Here we report the structure of an agonist-bound, active state of the human M2 muscarinic acetylcholine receptor stabilized by a G-protein mimetic camelid antibody fragment isolated by conformational selection using yeast surface display. In addition to the expected changes in the intracellular surface, the structure reveals larger conformational changes in the extracellular region and orthosteric binding site than observed in the active states of the β2AR and rhodopsin. We also report the structure of the M2 receptor simultaneously bound to the orthosteric agonist iperoxo and the positive allosteric modulator LY2119620. This structure reveals that LY2119620 recognizes a largely pre-formed binding site in the extracellular vestibule of the iperoxo-bound receptor, inducing a slight contraction of this outer binding pocket. These structures offer important insights into the activation mechanism and allosteric modulation of muscarinic receptors. More... »

PAGES

101

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature12735

DOI

http://dx.doi.org/10.1038/nature12735

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1037825045

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/24256733


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