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Conformational Flexibility and Structural Dynamics in GPCR-Mediated G Protein Activation: A Perspective
Open accessAbstract
Structure and dynamics of G proteins and their cognate receptors, both alone and in complex, are becoming increasingly accessible to experimental techniques. Understanding the conformational changes and timelines that govern these changes can lead to new insights into the processes of ligand binding and associated G protein activation. Experimental systems may involve the use of, or otherwise stabilize, non-native environments. This can complicate our understanding of structural and dynamic features of processes such as the ionic lock, tryptophan toggle, and G protein flexibility. While elements in the receptor's transmembrane helices and the C-terminal α5 helix of Gα undergo well-defined structural changes, regions subject to conformational flexibility may be important in fine-tuning the interactions between activated receptors and G proteins. The pairing of computational and experimental approaches will continue to provide powerful tools to probe the conformation and dynamics of receptor-mediated G protein activation.
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Metadata
- Authors
- Preininger, A. M., Meiler, J., & Hamm, H. E.
- Affiliations
- Vanderbilt University Medical Center (US)
- Vanderbilt University (US)
- Corresponding author
- Preininger, Anita M.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2013-07
- Volume
- 425
- Issue
- 13
- Pages
- 2288-2298
- ISSN
- 0022-2836 (ISSN-L)
- PMC
- PMC3686903
- OpenAlex
- W2064856742
- Cited by
- 104
- References
- 90
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 3 · 2023: 7 · 2022: 6 · 2021: 5 · 2020: 5 · 2019: 11 · 2018: 9 · 2017: 5 · 2016: 6 · 2015: 15 · 2014: 17 · 2013: 5
- FWCI
- 1.35
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Mental Health (MH090192, R01MH090192)
- National Eye Institute (EY006062, R01EY006062)
- National Institute of General Medical Sciences (R01GM095633, R01GM099842, R01GM080403, GM 080403, GM099842, GM095633)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK097376)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- G protein-coupled receptors, G protein activation, conformational flexibility, structural dynamics, ligand binding, ionic lock, transmembrane helices, receptor-G protein interaction
- MeSH terms
- Allosteric Regulation, Models, Molecular, Protein Conformation, Signal Transduction, Crystallography, X-Ray, GTP-Binding Proteins, Receptors, G-Protein-Coupled, Molecular Dynamics Simulation
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