An online resource for GPCR structure determination and analysis

Research output: Contribution to journal › Review › Research › peer-review

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An online resource for GPCR structure determination and analysis. / Munk, Christian; Mutt, Eshita; Isberg, Vignir; Nikolajsen, Louise F; Bibbe, Janne M; Flock, Tilman; Hanson, Michael A; Stevens, Raymond C; Deupi, Xavier; Gloriam, David E.

In: Nature Methods, Vol. 16, No. 2, 2019, p. 151-162.

Research output: Contribution to journal › Review › Research › peer-review

Harvard

Munk, C, Mutt, E, Isberg, V, Nikolajsen, LF, Bibbe, JM, Flock, T, Hanson, MA, Stevens, RC, Deupi, X & Gloriam, DE 2019, 'An online resource for GPCR structure determination and analysis', Nature Methods, vol. 16, no. 2, pp. 151-162. https://doi.org/10.1038/s41592-018-0302-x

APA

Munk, C., Mutt, E., Isberg, V., Nikolajsen, L. F., Bibbe, J. M., Flock, T., Hanson, M. A., Stevens, R. C., Deupi, X., & Gloriam, D. E. (2019). An online resource for GPCR structure determination and analysis. Nature Methods, 16(2), 151-162. https://doi.org/10.1038/s41592-018-0302-x

Vancouver

Munk C, Mutt E, Isberg V, Nikolajsen LF, Bibbe JM, Flock T et al. An online resource for GPCR structure determination and analysis. Nature Methods. 2019;16(2):151-162. https://doi.org/10.1038/s41592-018-0302-x

Author

Munk, Christian ; Mutt, Eshita ; Isberg, Vignir ; Nikolajsen, Louise F ; Bibbe, Janne M ; Flock, Tilman ; Hanson, Michael A ; Stevens, Raymond C ; Deupi, Xavier ; Gloriam, David E. / An online resource for GPCR structure determination and analysis. In: Nature Methods. 2019 ; Vol. 16, No. 2. pp. 151-162.

Bibtex

@article{ec9be93f134943d8ab9fdb90cf81052a,
title = "An online resource for GPCR structure determination and analysis",
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.",
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",
author = "Christian Munk and Eshita Mutt and Vignir Isberg and Nikolajsen, {Louise F} and Bibbe, {Janne M} and Tilman Flock and Hanson, {Michael A} and Stevens, {Raymond C} and Xavier Deupi and Gloriam, {David E}",
year = "2019",
doi = "10.1038/s41592-018-0302-x",
language = "English",
volume = "16",
pages = "151--162",
journal = "Nature Methods",
issn = "1548-7091",
publisher = "nature publishing group",
number = "2",

}

RIS

TY - JOUR

T1 - An online resource for GPCR structure determination and analysis

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

PY - 2019

Y1 - 2019

N2 - 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.

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

VL - 16

SP - 151

EP - 162

JO - Nature Methods

JF - Nature Methods

SN - 1548-7091

IS - 2

ER -

ID: 227424411