How do molecular dynamics data complement static structural data of GPCRs
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- dc.contributor.author Torrens Fontanals, Mariona
- dc.contributor.author Stepniewski, Tomasz Maciej, 1988-
- dc.contributor.author Aranda García, David
- dc.contributor.author Morales Pastor, Adrián
- dc.contributor.author Medel Lacruz, Brian
- dc.contributor.author Selent, Jana
- dc.date.accessioned 2020-09-23T06:03:01Z
- dc.date.available 2020-09-23T06:03:01Z
- dc.date.issued 2020
- dc.description.abstract G protein-coupled receptors (GPCRs) are implicated in nearly every physiological process in the human body and therefore represent an important drug targeting class. Advances in X-ray crystallography and cryo-electron microscopy (cryo-EM) have provided multiple static structures of GPCRs in complex with various signaling partners. However, GPCR functionality is largely determined by their flexibility and ability to transition between distinct structural conformations. Due to this dynamic nature, a static snapshot does not fully explain the complexity of GPCR signal transduction. Molecular dynamics (MD) simulations offer the opportunity to simulate the structural motions of biological processes at atomic resolution. Thus, this technique can incorporate the missing information on protein flexibility into experimentally solved structures. Here, we review the contribution of MD simulations to complement static structural data and to improve our understanding of GPCR physiology and pharmacology, as well as the challenges that still need to be overcome to reach the full potential of this technique.
- dc.format.mimetype application/pdf
- dc.identifier.citation Torrens-Fontanals M, Stepniewski TM, Aranda-García D, Morales-Pastor A, Medel-Lacruz B, Selent J. How do molecular dynamics data complement static structural data of GPCRs. Int J Mol Sci. 2020; 21(16):5933. DOI: 10.3390/ijms21165933
- dc.identifier.doi http://dx.doi.org/10.3390/ijms21165933
- dc.identifier.issn 1422-0067
- dc.identifier.uri http://hdl.handle.net/10230/45330
- dc.language.iso eng
- dc.publisher MDPI
- dc.relation.ispartof Int J Mol Sci. 2020; 21(16):5933
- dc.rights © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
- dc.rights.accessRights info:eu-repo/semantics/openAccess
- dc.rights.uri http://creativecommons.org/licenses/by/4.0/
- dc.subject.keyword GPCRs
- dc.subject.keyword Drug discovery
- dc.subject.keyword Ligand binding
- dc.subject.keyword Molecular dynamics
- dc.subject.keyword Receptor (in)activation
- dc.subject.keyword Receptor signaling
- dc.title How do molecular dynamics data complement static structural data of GPCRs
- dc.type info:eu-repo/semantics/article
- dc.type.version info:eu-repo/semantics/publishedVersion