Molecular signatures of G-protein-coupled receptors

By A. Venkatakrishnan, X. Deupí, G. Lebon, C. Tate, G. Schertler, M. Babu. Nature, 2013

1,466 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology, Radiology, Nuclear Medicine and Imaging

View Paper: https://www.semanticscholar.org/paper/e8dbc736754b279f30fda353f9c7c06fa66d49bb

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cellular and Molecular Neuroscience

In Molecular Biology

In Radiology, Nuclear Medicine and Imaging

Citations in the corpus

5-HT2C Receptor Structures Reveal the Structural Basis of GPCR Polypharmacology (2018, positive): “Compared to the ERG-bound structure, RIT binds approximately one helical turn deeper into the TM bundle (Figure 2B), which is outside of the recognized orthosteric site of other solved aminergic GPCR structures (Venkatakrishnan et al., 2013).”
A Structural Framework for GPCR Chemogenomics: What's In a Residue Number? (2018, background): “Residues F and F do not interact with any of the class A GPCR crystal structures that have been reported so far, but have been shown to play an important role in the activation mechanism of class A GPCRs [38, 43, 62].”
GPCRdb: the G protein‐coupled receptor database – an introduction (2016, background): “…for the 7TM of all classes but B2/adhesions and T/taste2 and have revealed common conformational changes during receptor activation, allosteric modulation by ions, lipids, cholesterol, and water; as well as G protein binding (Katritch et al., 2013; Venkatakrishnan et al., 2013; Tehan et al., 2014).”
GPCR-SSFE 2.0—a fragment-based molecular modeling web tool for Class A G-protein coupled receptors (2017, background): “Despite recent advances in stabilizing and crystallizing GPCRs, it is still difficult to obtain experimental structures of them (4).”
Structures of signaling complexes of lipid receptors S1PR1 and S1PR5 reveal mechanisms of activation and drug recognition (2021, background): “In addition to the TM domains, the cytoplasmic loops, particularly ICL2 and ICL3, are postulated to contribute to G protein interactions following activation.(39) In our structural comparison, the ICL2 region in S1PR1 packs against the α5 helix more tightly than that observed for S1PR5, and detailed”
Integrating structural and mutagenesis data to elucidate GPCR ligand binding (2016, background): “com changes during receptor activation, allosteric modulation by ligands, ions and lipids, cholesterol, as well as G protein binding [5 ,6 ,7].”
GPCR-ModSim: A comprehensive web based solution for modeling G-protein coupled receptors (2016, methodology): “The other new feature is the refinement of our MD equilibration protocol which now uses a network of pair-distance restraints, derived from a comprehensive analysis of GPCR crystal structures (18).”