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 journal › Review › Research › peer-review
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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
C2 - 29576399
AN - SCOPUS:85044290949
VL - 39
SP - 494
EP - 512
JO - Trends in Pharmacological Sciences
JF - Trends in Pharmacological Sciences
SN - 0165-6147
IS - 5
ER -
ID: 199351571