An Online Resource for GPCR Structure Determination and Analysis

By Christian Munk, Eshita Mutt, Vignir Ísberg, Louise F. Nikolajsen, J. M. Bibbe, T. Flock, M. Hanson, Raymond C. Stevens, X. Deupí, David E. Gloriam. 2019

118 citations recorded by the source corpus.

G-protein-coupled receptors (GPCRs) transduce physiological and sensory stimuli into appropriate cellular responses and mediate the actions of one-third of drugs. GPCR structural studies have revealed the general bases of receptor activation, signaling, drug action and allosteric modulation, but so far cover only 13% of nonolfactory receptors. We broadly surveyed the receptor modifications/engineering and methods used to produce all available GPCR crystal and cryo-electron microscopy (cryo-EM) structures, and present an interactive resource integrated in GPCRdb (http://www.gpcrdb.org) to assist users in designing constructs and browsing appropriate experimental conditions for structure studies. An interactive online resource integrated in the GPCRdb hub presents tools to design GPCR constructs and determine appropriate experimental conditions for structural studies by crystallography and cryo-EM.

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

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Citations in the corpus

GPCRdb in 2021: integrating GPCR sequence, structure and function (2020, methodology): “Furthermore, GPCRdb has data driven tools to identify sequence signatures of functional residue determinants (see below), to mutate ligand binding sites (27) and to design constructs and experiments for structure determination (12).”
GPCRdb in 2023: state-specific structure models using AlphaFold2 and new ligand resources (2022, methodology): “Data-driven experiment design tools: The current set of data-driven tools serve to (i) design constructs for crystallography/cryo-EM studies (28), (ii) identify functional determinants from comparative sequence analysis, (iii) provide mutations stabilizing inactive/active states, and mutate ligand b”
Structure and dynamics of the CGRP receptor in apo and peptide-bound forms (2021, background): “There has been considerable success in obtaining inactive-state structures bound to inhibitor ligands, in particular through the x-ray crystallography of engineered GPCRs (3, 4).”
AlphaFold2 versus experimental structures: evaluation on G protein-coupled receptors (2022, methodology): “org/structure/) according to the open degree of the TM6 helix [39, 40].”