@inproceedings{87a8aed398aa4f7cbf8da940661d2940,
title = "Informed development of drugs acting at Family B G protein-coupled receptors",
abstract = "Rational refinement and development of receptor-active ligands can come from high-resolution insights into the structures of these potential drug targets. Structural insights for Family A G protein-coupled receptors (GPCRs) have been advanced substantially with the recently reported crystal structure of the intact β2-adrenergic receptor. While high-resolution structural insights for Family B GPCRs are also advancing, this is currently limited to the functionally important extracellular amino-terminal tail domain of those receptors. The current report describes how these structures can provide leads for the development of small-molecule agonist drugs acting at Family B GPCRs. Endogenous agonist activity within the amino terminus of these receptors could be key for the development of such drugs.",
keywords = "Activation mechanisms, G protein-coupled receptors, Ligand binding, Receptor structure, Secretin receptor",
author = "Miller, {Laurence J.}",
note = "Copyright: Copyright 2018 Elsevier B.V., All rights reserved.",
year = "2008",
month = nov,
doi = "10.1196/annals.1418.001",
language = "English (US)",
isbn = "9781573317047",
series = "Annals of the New York Academy of Sciences",
publisher = "Blackwell Publishing Inc.",
pages = "203--209",
booktitle = "Neural Signaling Opportunities for Novel Diagnostic Approaches and Therapies",
}