Definition of the G protein-coupled receptor transmembrane bundle binding pocket and calculation of receptor similarities for drug design

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Definition of the G protein-coupled receptor transmembrane bundle binding pocket and calculation of receptor similarities for drug design. / Gloriam, David Erik Immanuel; Foord, Steven M; Blaney, Frank E; Garland, Stephen L.

In: Journal of Medicinal Chemistry, Vol. 52, No. 14, 2009, p. 4429-4442.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Gloriam, DEI, Foord, SM, Blaney, FE & Garland, SL 2009, 'Definition of the G protein-coupled receptor transmembrane bundle binding pocket and calculation of receptor similarities for drug design', Journal of Medicinal Chemistry, vol. 52, no. 14, pp. 4429-4442. https://doi.org/10.1021/jm900319e

APA

Gloriam, D. E. I., Foord, S. M., Blaney, F. E., & Garland, S. L. (2009). Definition of the G protein-coupled receptor transmembrane bundle binding pocket and calculation of receptor similarities for drug design. Journal of Medicinal Chemistry, 52(14), 4429-4442. https://doi.org/10.1021/jm900319e

Vancouver

Gloriam DEI, Foord SM, Blaney FE, Garland SL. Definition of the G protein-coupled receptor transmembrane bundle binding pocket and calculation of receptor similarities for drug design. Journal of Medicinal Chemistry. 2009;52(14):4429-4442. https://doi.org/10.1021/jm900319e

Author

Gloriam, David Erik Immanuel ; Foord, Steven M ; Blaney, Frank E ; Garland, Stephen L. / Definition of the G protein-coupled receptor transmembrane bundle binding pocket and calculation of receptor similarities for drug design. In: Journal of Medicinal Chemistry. 2009 ; Vol. 52, No. 14. pp. 4429-4442.

Bibtex

@article{8ccde8309bd811df928f000ea68e967b,
title = "Definition of the G protein-coupled receptor transmembrane bundle binding pocket and calculation of receptor similarities for drug design",
abstract = "Recent advances in structural biology for G-protein-coupled receptors (GPCRs) have provided new opportunities to improve the definition of the transmembrane binding pocket. Here a reference set of 44 residue positions accessible for ligand binding was defined through detailed analysis of all currently available crystal structures. This was used to characterize pharmacological relationships of Family A/Rhodopsin family GPCRs, minimizing evolutionary influence from parts of the receptor that do not generally affect ligand binding. The resultant dendogram tended to group receptors according to endogenous ligand types, although it revealed subdivision of certain classes, notably peptide and lipid receptors. The transmembrane binding site reference set, particularly when coupled with a means of identifying the subset of ligand binding residues, provides a general paradigm for understanding the pharmacology/selectivity profile of ligands at Family A GPCRs. This has wide applicability to GPCR drug design problems across many disease areas.",
keywords = "The Faculty of Pharmaceutical Sciences",
author = "Gloriam, {David Erik Immanuel} and Foord, {Steven M} and Blaney, {Frank E} and Garland, {Stephen L}",
note = "Keywords: Amino Acid Sequence; Binding Sites; Cell Membrane; Drug Design; Humans; Ligands; Lipid Metabolism; Melatonin; Molecular Sequence Data; Opsins; Peptides; Receptors, G-Protein-Coupled; Receptors, Proteinase-Activated; Receptors, Purinergic P1; Retinaldehyde; Rhodopsin; Sequence Alignment",
year = "2009",
doi = "10.1021/jm900319e",
language = "English",
volume = "52",
pages = "4429--4442",
journal = "Journal of Medicinal Chemistry",
issn = "0022-2623",
publisher = "American Chemical Society",
number = "14",

}

RIS

TY - JOUR

T1 - Definition of the G protein-coupled receptor transmembrane bundle binding pocket and calculation of receptor similarities for drug design

AU - Gloriam, David Erik Immanuel

AU - Foord, Steven M

AU - Blaney, Frank E

AU - Garland, Stephen L

N1 - Keywords: Amino Acid Sequence; Binding Sites; Cell Membrane; Drug Design; Humans; Ligands; Lipid Metabolism; Melatonin; Molecular Sequence Data; Opsins; Peptides; Receptors, G-Protein-Coupled; Receptors, Proteinase-Activated; Receptors, Purinergic P1; Retinaldehyde; Rhodopsin; Sequence Alignment

PY - 2009

Y1 - 2009

N2 - Recent advances in structural biology for G-protein-coupled receptors (GPCRs) have provided new opportunities to improve the definition of the transmembrane binding pocket. Here a reference set of 44 residue positions accessible for ligand binding was defined through detailed analysis of all currently available crystal structures. This was used to characterize pharmacological relationships of Family A/Rhodopsin family GPCRs, minimizing evolutionary influence from parts of the receptor that do not generally affect ligand binding. The resultant dendogram tended to group receptors according to endogenous ligand types, although it revealed subdivision of certain classes, notably peptide and lipid receptors. The transmembrane binding site reference set, particularly when coupled with a means of identifying the subset of ligand binding residues, provides a general paradigm for understanding the pharmacology/selectivity profile of ligands at Family A GPCRs. This has wide applicability to GPCR drug design problems across many disease areas.

AB - Recent advances in structural biology for G-protein-coupled receptors (GPCRs) have provided new opportunities to improve the definition of the transmembrane binding pocket. Here a reference set of 44 residue positions accessible for ligand binding was defined through detailed analysis of all currently available crystal structures. This was used to characterize pharmacological relationships of Family A/Rhodopsin family GPCRs, minimizing evolutionary influence from parts of the receptor that do not generally affect ligand binding. The resultant dendogram tended to group receptors according to endogenous ligand types, although it revealed subdivision of certain classes, notably peptide and lipid receptors. The transmembrane binding site reference set, particularly when coupled with a means of identifying the subset of ligand binding residues, provides a general paradigm for understanding the pharmacology/selectivity profile of ligands at Family A GPCRs. This has wide applicability to GPCR drug design problems across many disease areas.

KW - The Faculty of Pharmaceutical Sciences

U2 - 10.1021/jm900319e

DO - 10.1021/jm900319e

M3 - Journal article

VL - 52

SP - 4429

EP - 4442

JO - Journal of Medicinal Chemistry

JF - Journal of Medicinal Chemistry

SN - 0022-2623

IS - 14

ER -

ID: 21087812