Chemical Diversity in the G Protein-Coupled Receptor Superfamily

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Chemical Diversity in the G Protein-Coupled Receptor Superfamily. / Vass, Márton; Kooistra, Albert J.; Yang, Dehua; Stevens, Raymond C.; Wang, Ming Wei; de Graaf, Chris.

In: Trends in Pharmacological Sciences, Vol. 39, No. 5, 01.05.2018, p. 494-512.

Research output: Contribution to journalReviewResearchpeer-review

Harvard

Vass, M, Kooistra, AJ, Yang, D, Stevens, RC, Wang, MW & de Graaf, C 2018, 'Chemical Diversity in the G Protein-Coupled Receptor Superfamily', Trends in Pharmacological Sciences, vol. 39, no. 5, pp. 494-512. https://doi.org/10.1016/j.tips.2018.02.004

APA

Vass, M., Kooistra, A. J., Yang, D., Stevens, R. C., Wang, M. W., & de Graaf, C. (2018). Chemical Diversity in the G Protein-Coupled Receptor Superfamily. Trends in Pharmacological Sciences, 39(5), 494-512. https://doi.org/10.1016/j.tips.2018.02.004

Vancouver

Vass M, Kooistra AJ, Yang D, Stevens RC, Wang MW, de Graaf C. Chemical Diversity in the G Protein-Coupled Receptor Superfamily. Trends in Pharmacological Sciences. 2018 May 1;39(5):494-512. https://doi.org/10.1016/j.tips.2018.02.004

Author

Vass, Márton ; Kooistra, Albert J. ; Yang, Dehua ; Stevens, Raymond C. ; Wang, Ming Wei ; de Graaf, Chris. / Chemical Diversity in the G Protein-Coupled Receptor Superfamily. In: Trends in Pharmacological Sciences. 2018 ; Vol. 39, No. 5. pp. 494-512.

Bibtex

@article{fd514dba929e4d64b2f5fa334256a81d,
title = "Chemical Diversity in the G Protein-Coupled Receptor Superfamily",
abstract = "G protein-coupled receptors (GPCRs) are the largest family of cell signaling transmembrane proteins that can be modulated by a plethora of chemical compounds. Systematic cheminformatics analysis of structurally and pharmacologically characterized GPCR ligands shows that cocrystallized GPCR ligands cover a significant part of chemical ligand space, despite their limited number. Many GPCR ligands and substructures interact with multiple receptors, providing a basis for polypharmacological ligand design. Experimentally determined GPCR structures represent a variety of binding sites and receptor–ligand interactions that can be translated to chemically similar ligands for which structural data are lacking. This integration of structural, pharmacological, and chemical information on GPCR–ligand interactions enables the extension of the structural GPCR–ligand interactome and the structure-based design of novel modulators of GPCR function.",
keywords = "G protein-coupled receptor (GPCR), structural cheminformatics",
author = "M{\'a}rton Vass and Kooistra, {Albert J.} and Dehua Yang and Stevens, {Raymond C.} and Wang, {Ming Wei} and {de Graaf}, Chris",
year = "2018",
month = "5",
day = "1",
doi = "10.1016/j.tips.2018.02.004",
language = "English",
volume = "39",
pages = "494--512",
journal = "Trends in Pharmacological Sciences",
issn = "0165-6147",
publisher = "Elsevier Ltd. * Trends Journals",
number = "5",

}

RIS

TY - JOUR

T1 - Chemical Diversity in the G Protein-Coupled Receptor Superfamily

AU - Vass, Márton

AU - Kooistra, Albert J.

AU - Yang, Dehua

AU - Stevens, Raymond C.

AU - Wang, Ming Wei

AU - de Graaf, Chris

PY - 2018/5/1

Y1 - 2018/5/1

N2 - G protein-coupled receptors (GPCRs) are the largest family of cell signaling transmembrane proteins that can be modulated by a plethora of chemical compounds. Systematic cheminformatics analysis of structurally and pharmacologically characterized GPCR ligands shows that cocrystallized GPCR ligands cover a significant part of chemical ligand space, despite their limited number. Many GPCR ligands and substructures interact with multiple receptors, providing a basis for polypharmacological ligand design. Experimentally determined GPCR structures represent a variety of binding sites and receptor–ligand interactions that can be translated to chemically similar ligands for which structural data are lacking. This integration of structural, pharmacological, and chemical information on GPCR–ligand interactions enables the extension of the structural GPCR–ligand interactome and the structure-based design of novel modulators of GPCR function.

AB - G protein-coupled receptors (GPCRs) are the largest family of cell signaling transmembrane proteins that can be modulated by a plethora of chemical compounds. Systematic cheminformatics analysis of structurally and pharmacologically characterized GPCR ligands shows that cocrystallized GPCR ligands cover a significant part of chemical ligand space, despite their limited number. Many GPCR ligands and substructures interact with multiple receptors, providing a basis for polypharmacological ligand design. Experimentally determined GPCR structures represent a variety of binding sites and receptor–ligand interactions that can be translated to chemically similar ligands for which structural data are lacking. This integration of structural, pharmacological, and chemical information on GPCR–ligand interactions enables the extension of the structural GPCR–ligand interactome and the structure-based design of novel modulators of GPCR function.

KW - G protein-coupled receptor (GPCR)

KW - structural cheminformatics

UR - http://www.scopus.com/inward/record.url?scp=85044290949&partnerID=8YFLogxK

U2 - 10.1016/j.tips.2018.02.004

DO - 10.1016/j.tips.2018.02.004

M3 - Review

VL - 39

SP - 494

EP - 512

JO - Trends in Pharmacological Sciences

JF - Trends in Pharmacological Sciences

SN - 0165-6147

IS - 5

ER -

ID: 199351571