Structural Mapping of Adenosine Receptor Mutations

Department of Drug Design and Pharmacology

Structural Mapping of Adenosine Receptor Mutations: Ligand Binding and Signaling Mechanisms

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

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Structural Mapping of Adenosine Receptor Mutations : Ligand Binding and Signaling Mechanisms. / Jespers, Willem; Schiedel, Anke C; Heitman, Laura H; Cooke, Robert M; Kleene, Lisa; van Westen, Gerard J P; Gloriam, David E; Müller, Christa E; Sotelo, Eddy; Gutiérrez-de-Terán, Hugo.

In: Trends in Pharmacological Sciences, Vol. 39, No. 1, 01.2018, p. 75-89.

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

Harvard

Jespers, W, Schiedel, AC, Heitman, LH, Cooke, RM, Kleene, L, van Westen, GJP, Gloriam, DE, Müller, CE, Sotelo, E & Gutiérrez-de-Terán, H 2018, 'Structural Mapping of Adenosine Receptor Mutations: Ligand Binding and Signaling Mechanisms', Trends in Pharmacological Sciences, vol. 39, no. 1, pp. 75-89. https://doi.org/10.1016/j.tips.2017.11.001

APA

Jespers, W., Schiedel, A. C., Heitman, L. H., Cooke, R. M., Kleene, L., van Westen, G. J. P., Gloriam, D. E., Müller, C. E., Sotelo, E., & Gutiérrez-de-Terán, H. (2018). Structural Mapping of Adenosine Receptor Mutations: Ligand Binding and Signaling Mechanisms. Trends in Pharmacological Sciences, 39(1), 75-89. https://doi.org/10.1016/j.tips.2017.11.001

Vancouver

Jespers W, Schiedel AC, Heitman LH, Cooke RM, Kleene L, van Westen GJP et al. Structural Mapping of Adenosine Receptor Mutations: Ligand Binding and Signaling Mechanisms. Trends in Pharmacological Sciences. 2018 Jan;39(1):75-89. https://doi.org/10.1016/j.tips.2017.11.001

Author

Jespers, Willem ; Schiedel, Anke C ; Heitman, Laura H ; Cooke, Robert M ; Kleene, Lisa ; van Westen, Gerard J P ; Gloriam, David E ; Müller, Christa E ; Sotelo, Eddy ; Gutiérrez-de-Terán, Hugo. / Structural Mapping of Adenosine Receptor Mutations : Ligand Binding and Signaling Mechanisms. In: Trends in Pharmacological Sciences. 2018 ; Vol. 39, No. 1. pp. 75-89.

Bibtex

@article{09d884fcea964ab1bf2fa5db24610421,

title = "Structural Mapping of Adenosine Receptor Mutations: Ligand Binding and Signaling Mechanisms",

abstract = "The four adenosine receptors (ARs), A1, A2A, A2B, and A3, constitute a subfamily of G protein-coupled receptors (GPCRs) with exceptional foundations for structure-based ligand design. The vast amount of mutagenesis data, accumulated in the literature since the 1990s, has been recently supplemented with structural information, currently consisting of several inactive and active structures of the A2A and inactive conformations of the A1 ARs. We provide the first integrated view of the pharmacological, biochemical, and structural data available for this receptor family, by mapping onto the relevant crystal structures all site-directed mutagenesis data, curated and deposited at the GPCR database (available through http://www.gpcrdb.org). This analysis provides novel insights into ligand binding, allosteric modulation, and signaling of the AR family.",

keywords = "Journal Article, Review",

author = "Willem Jespers and Schiedel, {Anke C} and Heitman, {Laura H} and Cooke, {Robert M} and Lisa Kleene and {van Westen}, {Gerard J P} and Gloriam, {David E} and M{\"u}ller, {Christa E} and Eddy Sotelo and Hugo Guti{\'e}rrez-de-Ter{\'a}n",

year = "2018",

month = jan,

doi = "10.1016/j.tips.2017.11.001",

language = "English",

volume = "39",

pages = "75--89",

journal = "Trends in Pharmacological Sciences",

issn = "0165-6147",

publisher = "Elsevier Ltd. * Trends Journals",

number = "1",

}

RIS

TY - JOUR

T1 - Structural Mapping of Adenosine Receptor Mutations

T2 - Ligand Binding and Signaling Mechanisms

AU - Jespers, Willem

AU - Schiedel, Anke C

AU - Heitman, Laura H

AU - Cooke, Robert M

AU - Kleene, Lisa

AU - van Westen, Gerard J P

AU - Gloriam, David E

AU - Müller, Christa E

AU - Sotelo, Eddy

AU - Gutiérrez-de-Terán, Hugo

PY - 2018/1

Y1 - 2018/1

N2 - The four adenosine receptors (ARs), A1, A2A, A2B, and A3, constitute a subfamily of G protein-coupled receptors (GPCRs) with exceptional foundations for structure-based ligand design. The vast amount of mutagenesis data, accumulated in the literature since the 1990s, has been recently supplemented with structural information, currently consisting of several inactive and active structures of the A2A and inactive conformations of the A1 ARs. We provide the first integrated view of the pharmacological, biochemical, and structural data available for this receptor family, by mapping onto the relevant crystal structures all site-directed mutagenesis data, curated and deposited at the GPCR database (available through http://www.gpcrdb.org). This analysis provides novel insights into ligand binding, allosteric modulation, and signaling of the AR family.

AB - The four adenosine receptors (ARs), A1, A2A, A2B, and A3, constitute a subfamily of G protein-coupled receptors (GPCRs) with exceptional foundations for structure-based ligand design. The vast amount of mutagenesis data, accumulated in the literature since the 1990s, has been recently supplemented with structural information, currently consisting of several inactive and active structures of the A2A and inactive conformations of the A1 ARs. We provide the first integrated view of the pharmacological, biochemical, and structural data available for this receptor family, by mapping onto the relevant crystal structures all site-directed mutagenesis data, curated and deposited at the GPCR database (available through http://www.gpcrdb.org). This analysis provides novel insights into ligand binding, allosteric modulation, and signaling of the AR family.

KW - Journal Article

KW - Review

U2 - 10.1016/j.tips.2017.11.001

DO - 10.1016/j.tips.2017.11.001

M3 - Review

C2 - 29203139

VL - 39

SP - 75

EP - 89

JO - Trends in Pharmacological Sciences

JF - Trends in Pharmacological Sciences

SN - 0165-6147

IS - 1

ER -

ID: 186867144