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An online resource for GPCR structure determination and analysis.

  • Munk C Department of Drug Design and Pharmacology, University of Copenhagen, Copenhagen, Denmark. christian.munk@sund.ku.dk.
  • Mutt E Paul Scherrer Institute, Villigen, Switzerland.
  • Isberg V Department of Drug Design and Pharmacology, University of Copenhagen, Copenhagen, Denmark.
  • Nikolajsen LF Department of Drug Design and Pharmacology, University of Copenhagen, Copenhagen, Denmark.
  • Bibbe JM Department of Drug Design and Pharmacology, University of Copenhagen, Copenhagen, Denmark.
  • Flock T Paul Scherrer Institute, Villigen, Switzerland.
  • Hanson MA GPCR Consortium, San Marcos, CA, USA.
  • Stevens RC Departments of Biological Sciences and Chemistry, Bridge Institute, USC Michelson Center for Convergent Bioscience, University of Southern California, Los Angeles, CA, USA.
  • Deupi X Paul Scherrer Institute, Villigen, Switzerland.
  • Gloriam DE Department of Drug Design and Pharmacology, University of Copenhagen, Copenhagen, Denmark. david.gloriam@sund.ku.dk.
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  • 2019-01-22
Published in:
  • Nature methods. - 2019
Allosteric Site
Animals
Cattle
Computational Biology
Cryoelectron Microscopy
Crystallography, X-Ray
Databases, Protein
Drug Design
Glycosylation
HEK293 Cells
Humans
Internet
Mutation
Phosphorylation
Protein Domains
Protein Engineering
Receptors, G-Protein-Coupled
Rhodopsin
Signal Transduction
Software
English 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.
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  • English
Open access status
green
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Persistent URL
https://folia.unifr.ch/global/documents/173307
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