Recent advances in computational studies of GPCR-G protein interactions

View/ Open
Issue Date
2019-01-03Author
Wang, Jinan
Miao, Yinglong
Publisher
Elsevier
Type
Article
Article Version
Scholarly/refereed, author accepted manuscript
Rights
Copyright © 2019 Elsevier Inc. All rights reserved.
Metadata
Show full item recordAbstract
Protein-protein interactions are key in cellular signaling. G protein-coupled receptors (GPCRs), the largest superfamily of human membrane proteins, are able to transduce extracellular signals (e.g., hormones and neurotransmitters) to intracellular proteins, in particular the G proteins. Since GPCRs serve as primary targets of ~ 1/3 of currently marketed drugs, it is important to understand mechanisms of GPCR signaling in order to design selective and potent drug molecules. This chapter focuses on recent advances in computational studies of the GPCR-G protein interactions using bioinformatics, protein-protein docking and molecular dynamics simulation approaches.
Description
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
Collections
Citation
Wang, J., & Miao, Y. (2019). Recent advances in computational studies of GPCR-G protein interactions. Advances in protein chemistry and structural biology, 116, 397–419. https://doi.org/10.1016/bs.apcsb.2018.11.011
Items in KU ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
We want to hear from you! Please share your stories about how Open Access to this item benefits YOU.
Except where otherwise noted, this item's license is described as: Copyright © 2019 Elsevier Inc. All rights reserved.
Related items
Showing items related by title, author, creator and subject.
-
Antiparallel Dimers of the Small Multidrug Resistance Protein EmrE Are More Stable Than Parallel Dimers
Lloris-Garcerá, Pilar; Bianchi, Frans; Slusky, Joanna; Seppälä, Susanna; Daley, Daniel O.; von Heijne, Gunnar (American Society for Biochemistry and Molecular Biology, 2012-06-14)The bacterial multidrug transporter EmrE is a dual-topology membrane protein and as such is able to insert into the membrane in two opposite orientations. The functional form of EmrE is a homodimer; however, the relative ... -
Selectivity by Small-Molecule Inhibitors of Protein Interactions Can Be Driven by Protein Surface Fluctuations
Johnson, David K.; Karanicolas, John (Public Library of Sciences, 2015-02-23)Small-molecules that inhibit interactions between specific pairs of proteins have long represented a promising avenue for therapeutic intervention in a variety of settings. Structural studies have shown that in many cases, ... -
Computational Design of Affinity and Specificity at Protein-Protein Interfaces
Karanicolas, John; Kuhlman, Brian (Elsevier, 2009-08)The computer-based design of protein-protein interactions is a rigorous test of our understanding of molecular recognition and an attractive approach for creating novel tools for cell and molecular research. Considerable ...