Abstract
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.
Original language | English |
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Journal | Nature Methods |
Volume | 16 |
Issue number | 2 |
Pages (from-to) | 151-162 |
ISSN | 1548-7091 |
DOIs | |
Publication status | Published - 2019 |
Keywords
- Allosteric Site
- Animals
- Cattle
- Computational Biology/methods
- Cryoelectron Microscopy
- Crystallography, X-Ray
- Databases, Protein
- Drug Design
- Glycosylation
- HEK293 Cells
- Humans
- Internet
- Mutation
- Phosphorylation
- Protein Domains
- Protein Engineering
- Receptors, G-Protein-Coupled/genetics
- Rhodopsin/chemistry
- Signal Transduction
- Software