Article

Thermodynamic Architecture and Conformational Plasticity of GPCRs

2022-11-27

Abstract excerpt

<h4>ABSTRACT</h4> G-protein-coupled receptors (GPCRs) are ubiquitous integral membrane proteins involved in diverse cellular signaling processes and consequently serve as crucial drug targets. Here, we carry out the first large-scale ensemble thermodynamic study of 45 different ligand-free GPCRs employing a structure-based statistical mechanical framework and identify extensive conformational plasticity encompass...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 817a9476-05d6-5279-a1f2-84073117e2db
DOI: 10.1101/2022.11.26.518034

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Thermodynamic Architecture and Conformational Plasticity of GPCRsDOI 10.1101/2022.11.26.518034Read

Conformational ensemble view of G protein-coupled receptors and the effect of mutations and ligand binding.Semantic proximity Read

Deciphering conformational selectivity in the A <sub>2A</sub> adenosine G protein-coupled receptor by Free Energy simulationsSemantic proximity Read

Elements and modulation of functional dynamics.Semantic proximity Read

Protein flexibility and dissociation pathway differentiation can explain onset of resistance mutations in kinasesSemantic proximity Read

Characterizing clinically relevant natural variants of GPCRs using computational approaches.Semantic proximity Read

Deep Learning Dynamic Allostery of G-Protein-Coupled ReceptorsSemantic proximity Read

Deep Learning Dynamic Allostery of G-Protein-Coupled ReceptorsSemantic proximity Read

Structural preferences shape the entropic force of disordered protein ensemblesSemantic proximity Read

Structural determinants of allosteric ligand activation in RXR heterodimers.Semantic proximity Read

Computational analysis of long-range allosteric communications in CFTRSemantic proximity Read

Hot-Spot Residues to be Mutated Common in G Protein-Coupled Receptors of Class A: Identification of Thermostabilizing Mutations Followed by Determination of Three-Dimensional Structures for Two Example Receptors.Semantic proximity Read

General structure-free energy relationships of hERG blocker binding under native cellular conditionsSemantic proximity Read