Principles of agonist recognition in Cys-loop receptors

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Principles of agonist recognition in Cys-loop receptors. / Lynagh, Timothy Peter; Pless, Stephan Alexander.

In: Frontiers in Physiology, Vol. 5, 160, 2014, p. 1-12.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Lynagh, TP & Pless, SA 2014, 'Principles of agonist recognition in Cys-loop receptors', Frontiers in Physiology, vol. 5, 160, pp. 1-12. https://doi.org/10.3389/fphys.2014.00160

APA

Lynagh, T. P., & Pless, S. A. (2014). Principles of agonist recognition in Cys-loop receptors. Frontiers in Physiology, 5, 1-12. [160]. https://doi.org/10.3389/fphys.2014.00160

Vancouver

Lynagh TP, Pless SA. Principles of agonist recognition in Cys-loop receptors. Frontiers in Physiology. 2014;5:1-12. 160. https://doi.org/10.3389/fphys.2014.00160

Author

Lynagh, Timothy Peter ; Pless, Stephan Alexander. / Principles of agonist recognition in Cys-loop receptors. In: Frontiers in Physiology. 2014 ; Vol. 5. pp. 1-12.

Bibtex

@article{da26ed75871c4632a141d815a74f1233,
title = "Principles of agonist recognition in Cys-loop receptors",
abstract = "Cys-loop receptors are ligand-gated ion channels that are activated by a structurally diverse array of neurotransmitters, including acetylcholine, serotonin, glycine, and GABA. After the term {"}chemoreceptor{"} emerged over 100 years ago, there was some wait until affinity labeling, molecular cloning, functional studies, and X-ray crystallography experiments identified the extracellular interface of adjacent subunits as the principal site of agonist binding. The question of how subtle differences at and around agonist-binding sites of different Cys-loop receptors can accommodate transmitters as chemically diverse as glycine and serotonin has been subject to intense research over the last three decades. This review outlines the functional diversity and current structural understanding of agonist-binding sites, including those of invertebrate Cys-loop receptors. Together, this provides a framework to understand the atomic determinants involved in how these valuable therapeutic targets recognize and bind their ligands.",
author = "Lynagh, {Timothy Peter} and Pless, {Stephan Alexander}",
year = "2014",
doi = "10.3389/fphys.2014.00160",
language = "English",
volume = "5",
pages = "1--12",
journal = "Frontiers in Physiology",
issn = "1664-042X",
publisher = "Frontiers Media S.A.",

}

RIS

TY - JOUR

T1 - Principles of agonist recognition in Cys-loop receptors

AU - Lynagh, Timothy Peter

AU - Pless, Stephan Alexander

PY - 2014

Y1 - 2014

N2 - Cys-loop receptors are ligand-gated ion channels that are activated by a structurally diverse array of neurotransmitters, including acetylcholine, serotonin, glycine, and GABA. After the term "chemoreceptor" emerged over 100 years ago, there was some wait until affinity labeling, molecular cloning, functional studies, and X-ray crystallography experiments identified the extracellular interface of adjacent subunits as the principal site of agonist binding. The question of how subtle differences at and around agonist-binding sites of different Cys-loop receptors can accommodate transmitters as chemically diverse as glycine and serotonin has been subject to intense research over the last three decades. This review outlines the functional diversity and current structural understanding of agonist-binding sites, including those of invertebrate Cys-loop receptors. Together, this provides a framework to understand the atomic determinants involved in how these valuable therapeutic targets recognize and bind their ligands.

AB - Cys-loop receptors are ligand-gated ion channels that are activated by a structurally diverse array of neurotransmitters, including acetylcholine, serotonin, glycine, and GABA. After the term "chemoreceptor" emerged over 100 years ago, there was some wait until affinity labeling, molecular cloning, functional studies, and X-ray crystallography experiments identified the extracellular interface of adjacent subunits as the principal site of agonist binding. The question of how subtle differences at and around agonist-binding sites of different Cys-loop receptors can accommodate transmitters as chemically diverse as glycine and serotonin has been subject to intense research over the last three decades. This review outlines the functional diversity and current structural understanding of agonist-binding sites, including those of invertebrate Cys-loop receptors. Together, this provides a framework to understand the atomic determinants involved in how these valuable therapeutic targets recognize and bind their ligands.

U2 - 10.3389/fphys.2014.00160

DO - 10.3389/fphys.2014.00160

M3 - Journal article

C2 - 24795655

VL - 5

SP - 1

EP - 12

JO - Frontiers in Physiology

JF - Frontiers in Physiology

SN - 1664-042X

M1 - 160

ER -

ID: 122597332