Unnatural amino acids as probes of ligand-receptor interactions and their conformational consequences

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

Standard

Unnatural amino acids as probes of ligand-receptor interactions and their conformational consequences. / Pless, Stephan Alexander; Ahern, Christopher A.

In: Annual Review of Pharmacology and Toxicology, Vol. 53, 2013, p. 211-29.

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

Harvard

Pless, SA & Ahern, CA 2013, 'Unnatural amino acids as probes of ligand-receptor interactions and their conformational consequences', Annual Review of Pharmacology and Toxicology, vol. 53, pp. 211-29. https://doi.org/10.1146/annurev-pharmtox-011112-140343

APA

Pless, S. A., & Ahern, C. A. (2013). Unnatural amino acids as probes of ligand-receptor interactions and their conformational consequences. Annual Review of Pharmacology and Toxicology, 53, 211-29. https://doi.org/10.1146/annurev-pharmtox-011112-140343

Vancouver

Pless SA, Ahern CA. Unnatural amino acids as probes of ligand-receptor interactions and their conformational consequences. Annual Review of Pharmacology and Toxicology. 2013;53:211-29. https://doi.org/10.1146/annurev-pharmtox-011112-140343

Author

Pless, Stephan Alexander ; Ahern, Christopher A. / Unnatural amino acids as probes of ligand-receptor interactions and their conformational consequences. In: Annual Review of Pharmacology and Toxicology. 2013 ; Vol. 53. pp. 211-29.

Bibtex

@article{5bd5ede6a0b541869886124f75e9e704,
title = "Unnatural amino acids as probes of ligand-receptor interactions and their conformational consequences",
abstract = "G protein-coupled receptors and ion channels couple a wide range of external stimuli to cellular growth and division, metabolism, motility, and a myriad of intra- and intercellular signaling pathways. G protein-coupled receptors initiate complex, interrelated downstream signaling cascades, whereas rapid ionic flux through channels directly supports membrane excitability and mediates cellular functions through second messengers. Because of these characteristics, these ubiquitous transmembrane proteins are valuable therapeutic targets and have provided fertile ground for the development of leading-edge synthetic and chemical biological approaches. Here we summarize recent advances in the use of site-directed incorporation of unnatural amino acids and chemical probes to study ligand-receptor interactions, determine the location of binding sites, and examine the downstream conformational consequences of ligand binding in G protein-coupled receptors and ion channels.",
keywords = "Amino Acids, Animals, Binding Sites, Humans, Ion Channels, Ligands, Membrane Proteins, Protein Conformation, Receptors, G-Protein-Coupled, Structure-Activity Relationship",
author = "Pless, {Stephan Alexander} and Ahern, {Christopher A}",
year = "2013",
doi = "10.1146/annurev-pharmtox-011112-140343",
language = "English",
volume = "53",
pages = "211--29",
journal = "Annual Review of Pharmacology and Toxicology",
issn = "0362-1642",
publisher = "Annual Reviews, inc.",

}

RIS

TY - JOUR

T1 - Unnatural amino acids as probes of ligand-receptor interactions and their conformational consequences

AU - Pless, Stephan Alexander

AU - Ahern, Christopher A

PY - 2013

Y1 - 2013

N2 - G protein-coupled receptors and ion channels couple a wide range of external stimuli to cellular growth and division, metabolism, motility, and a myriad of intra- and intercellular signaling pathways. G protein-coupled receptors initiate complex, interrelated downstream signaling cascades, whereas rapid ionic flux through channels directly supports membrane excitability and mediates cellular functions through second messengers. Because of these characteristics, these ubiquitous transmembrane proteins are valuable therapeutic targets and have provided fertile ground for the development of leading-edge synthetic and chemical biological approaches. Here we summarize recent advances in the use of site-directed incorporation of unnatural amino acids and chemical probes to study ligand-receptor interactions, determine the location of binding sites, and examine the downstream conformational consequences of ligand binding in G protein-coupled receptors and ion channels.

AB - G protein-coupled receptors and ion channels couple a wide range of external stimuli to cellular growth and division, metabolism, motility, and a myriad of intra- and intercellular signaling pathways. G protein-coupled receptors initiate complex, interrelated downstream signaling cascades, whereas rapid ionic flux through channels directly supports membrane excitability and mediates cellular functions through second messengers. Because of these characteristics, these ubiquitous transmembrane proteins are valuable therapeutic targets and have provided fertile ground for the development of leading-edge synthetic and chemical biological approaches. Here we summarize recent advances in the use of site-directed incorporation of unnatural amino acids and chemical probes to study ligand-receptor interactions, determine the location of binding sites, and examine the downstream conformational consequences of ligand binding in G protein-coupled receptors and ion channels.

KW - Amino Acids

KW - Animals

KW - Binding Sites

KW - Humans

KW - Ion Channels

KW - Ligands

KW - Membrane Proteins

KW - Protein Conformation

KW - Receptors, G-Protein-Coupled

KW - Structure-Activity Relationship

U2 - 10.1146/annurev-pharmtox-011112-140343

DO - 10.1146/annurev-pharmtox-011112-140343

M3 - Journal article

C2 - 23294309

VL - 53

SP - 211

EP - 229

JO - Annual Review of Pharmacology and Toxicology

JF - Annual Review of Pharmacology and Toxicology

SN - 0362-1642

ER -

ID: 122597503