An online resource for GPCR structure determination and analysis

Christian Munk; Eshita Mutt; Vignir Isberg; Louise F Nikolajsen; Janne M Bibbe; Tilman Flock; Michael A Hanson; Raymond C Stevens; Xavier Deupi; David E Gloriam

doi:10.1038/s41592-018-0302-x

An online resource for GPCR structure determination and analysis

Christian Munk, Eshita Mutt, Vignir Isberg, Louise F Nikolajsen, Janne M Bibbe, Tilman Flock, Michael A Hanson, Raymond C Stevens, Xavier Deupi, David E Gloriam

53 Citationer (Scopus)

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.

Originalsprog	Engelsk
Tidsskrift	Nature Methods
Vol/bind	16
Udgave nummer	2
Sider (fra-til)	151-162
Antal sider	12
ISSN	1548-7091
DOI	https://doi.org/10.1038/s41592-018-0302-x
Status	Udgivet - 1 feb. 2019

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10.1038/s41592-018-0302-x

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AU - Munk, Christian

AU - Mutt, Eshita

AU - Isberg, Vignir

AU - Nikolajsen, Louise F

AU - Bibbe, Janne M

AU - Flock, Tilman

AU - Hanson, Michael A

AU - Stevens, Raymond C

AU - Deupi, Xavier

AU - Gloriam, David E

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AB - 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.

KW - Allosteric Site

KW - Animals

KW - Cattle

KW - Computational Biology/methods

KW - Cryoelectron Microscopy

KW - Crystallography, X-Ray

KW - Databases, Protein

KW - Drug Design

KW - Glycosylation

KW - HEK293 Cells

KW - Humans

KW - Internet

KW - Mutation

KW - Phosphorylation

KW - Protein Domains

KW - Protein Engineering

KW - Receptors, G-Protein-Coupled/genetics

KW - Rhodopsin/chemistry

KW - Signal Transduction

KW - Software

U2 - 10.1038/s41592-018-0302-x

DO - 10.1038/s41592-018-0302-x

M3 - Review

C2 - 30664776

SN - 1548-7091

VL - 16

SP - 151

EP - 162

JO - Nature Methods

JF - Nature Methods

IS - 2

ER -

An online resource for GPCR structure determination and analysis

Abstract

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