ArticlePloS one2014
Differential stability of the crystallographic interfaces of mu- and kappa-opioid receptors.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 24 citations in OpenAlex.
- Co-Evolution of Opioid and Adrenergic Ligands and Receptors: Shared, Complementary Modules Explain Evolution of Functional Interactions and Suggest Novel Engineering Possibilities.Life (Basel, Switzerland) · 2021Article
- Computational Modeling of Claudin Structure and Function.International journal of molecular sciences · 2020Review
- Insights into the function of opioid receptors from molecular dynamics simulations of available crystal structures.British journal of pharmacology · 2018Review
- Closely related, yet unique: Distinct homo- and heterodimerization patterns of G protein coupled chemokine receptors and their fine-tuning by cholesterol.PLoS computational biology · 2018Article
- Article
- Conformational Heterogeneity of Intracellular Loop 3 of the μ-opioid G-protein Coupled Receptor.The journal of physical chemistry. B · 2016Article
- Molecular dynamics simulations and structure-based network analysis reveal structural and functional aspects of G-protein coupled receptor dimer interactions.Journal of computer-aided molecular design · 2016Article
- Understanding the fabric of protein crystals: computational classification of biological interfaces and crystal contacts.Bioinformatics (Oxford, England) · 2016Review
- Opioid receptors: Structural and mechanistic insights into pharmacology and signaling.European journal of pharmacology · 2015Review
- Preferred supramolecular organization and dimer interfaces of opioid receptors from simulated self-association.PLoS computational biology · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The recent mu-opioid receptor (MOPr) and kappa-opioid receptor (KOPr) crystal structures have inspired hypotheses of physiologically relevant dimerization contacts, specifically: a closely packed interface involving transmembrane (TM) helices TM5 and TM6, and a less compact interface, involving TM1, TM2, and helix 8 (H8). While the former was only found in MOPr crystals, similar arrangements of the latter were identified for both KOPr and MOPr. The relevance of these interfaces outside of a crystal lattice is called into question by the possibility that they might be influenced by the specific crystallization conditions. In this study, we have employed umbrella sampling molecular dynamics simulations of coarse-grained representations of the interacting MOPr or KOPr crystallographic structures, in the absence of the T4 lysozyme, and in an explicit lipid-water environment, to determine the strength of receptor dimerization at the different crystallographic interfaces. We note that the shape of the interface plays a dominant role in the strength of the interaction, and the pattern of contacting residues defines the shape of the potential of mean force. This information can be used to guide experiments aimed at exploring the role of dimerization in opioid receptor function.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.