Conformational complexity of G-protein-coupled receptors.

By Brian K. Kobilka, X. Deupí. TIPS - Trends in Pharmacological Sciences, 2007

710 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/b2e32b908113c255474761c018fcb4562f5250f9

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In Cellular and Molecular Neuroscience

In Molecular Biology

In Radiology, Nuclear Medicine and Imaging

Citations in the corpus

International Union of Basic and Clinical Pharmacology. LXXV. Nomenclature, Classification, and Pharmacology of G Protein-Coupled Melatonin Receptors (2010, background): “…in o ac id re si du es im po rt an t fo r m od u la ti n g bi n di n g to th e M T 1 re ce pt or (F ar ce et al ., 20 08 ). at A SPE T Journals on July 13, 2023 pharm rev.aspetjournals.org D ow nloaded from TM7, are major players in ligand binding (Kobilka and Deupi, 2007; Rosenbaum et al., 2007).”
Critical features for biosynthesis, stability, and functionality of a G protein-coupled receptor uncovered by all-versus-all mutations (2012, background): “Previous functional and structural studies on GPCRs have shown an important role for TM5 in receptor activation (1), because TM5 contains crucial residues that, upon binding of agonist, induce local structural rearrangements that presumably lock the receptor in the activated state (1, 20).”
Loss of constitutive activity is correlated with increased thermostability of the human adenosine A2A receptor (2013, background): “GPCRs exhibit significant conformational flexibility reflecting a number of functional states (Kobilka and Deupi, 2007).”
Molecular Mechanism of β-Arrestin-Biased Agonism at Seven-Transmembrane Receptors (2011, background): “Although the tremendous flexibility of 7TMRs in lipid bilayers (60, 61) implies that the conformational possibilities are enormous, these multiple active conformations are likely to share certain core features.”
Structure-Function of the G-protein-Coupled Receptor Superfamily (2012, background): “Distribution between states in ligand-free receptors can vary drastically, reflecting their different levels of basal activities (59, 60).”
GPCR Network: a large-scale collaboration on GPCR structure and function (2012, neutral): “This flexibility is essential for their activity under physio logical conditions 3 , but has made crystallization and structure determination using traditional methods very difficult.”
High-resolution atomic force microscopy and spectroscopy of native membrane proteins (2011, background): “Alterations in the interaction network of a membrane protein induced, for example, by ligand or inhibitor binding or (de-)protonation of functional groups can trigger conformational changes [232, 375].”
Activation mechanism of the β2-adrenergic receptor (2011, background): “Although the number of functionally distinct states and their conformations remain unknown, some are thought to be intermediates along the activation pathway (7, 9).”
Bridging Molecular Docking to Molecular Dynamics in Exploring Ligand-Protein Recognition Process: An Overview (2018, background): “These two apparently contrasting theories have simply diﬀerent ranges of applicability, and the descriptions they provide of molecular binding diﬀer for the chronological sequence of events in which the binding process is decomposed (Kobilka and Deupi, 2007; Okazaki and Takada, 2008; Zhou, 2010).”
The structure and function of G-protein-coupled receptors (2009, background): “Rather, they are more like molecular rheostats, able to sample a continuum of conformations with relatively closely spaced energie”