ArticleScientific reports2017
Structural heterogeneity of the μ-opioid receptor's conformational ensemble in the apo state.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 20 citations in OpenAlex.
- Dynamics of the Apo µ-Opioid Receptor in Complex with Gi Protein.International journal of molecular sciences · 2023Article
- Development of enhanced conformational sampling methods to probe the activation landscape of GPCRs.Advances in protein chemistry and structural biology · 2022Review
- Molecular insights into the biased signaling mechanism of the μ-opioid receptor.Molecular cell · 2021Article
- The G protein-first activation mechanism of opioid receptors by Gi protein and agonists.QRB discovery · 2021Article
- Exploring the activation pathway and GProceedings of the National Academy of Sciences of the United States of America · 2020Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
G-protein coupled receptors (GPCRs) are the largest and most pharmaceutically relevant family of membrane proteins. Here, fully unbiased, enhanced sampling simulations of a constitutively active mutant (CAM) of a class A GPCR, the μ-opioid receptor (μOR), demonstrates repeated transitions between the inactive (IS) and active-like (AS-L) states. The interconversion features typical activation/inactivation patterns involving established conformational rearrangements of conserved residues. By contrast, wild-type μOR remains in IS during the same course of simulation, consistent with the low basal activity of the protein. The simulations point to an important role of residue W293
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