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New Insights into the Structure and Function of Class B1 GPCRs
G protein–coupled receptors (GPCRs) are the largest family of cell surface receptors. Class B1 GPCRs constitute a subfamily of 15 receptors that characteristically contain large extracellular domains (ECDs) and respond to long polypeptide hormones. Class B1 GPCRs are critical regulators of homeostas...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10166269/ https://www.ncbi.nlm.nih.gov/pubmed/36546772 http://dx.doi.org/10.1210/endrev/bnac033 |
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author | Cary, Brian P Zhang, Xin Cao, Jianjun Johnson, Rachel M Piper, Sarah J Gerrard, Elliot J Wootten, Denise Sexton, Patrick M |
author_facet | Cary, Brian P Zhang, Xin Cao, Jianjun Johnson, Rachel M Piper, Sarah J Gerrard, Elliot J Wootten, Denise Sexton, Patrick M |
author_sort | Cary, Brian P |
collection | PubMed |
description | G protein–coupled receptors (GPCRs) are the largest family of cell surface receptors. Class B1 GPCRs constitute a subfamily of 15 receptors that characteristically contain large extracellular domains (ECDs) and respond to long polypeptide hormones. Class B1 GPCRs are critical regulators of homeostasis, and, as such, many are important drug targets. While most transmembrane proteins, including GPCRs, are recalcitrant to crystallization, recent advances in cryo-electron microscopy (cryo-EM) have facilitated a rapid expansion of the structural understanding of membrane proteins. As a testament to this success, structures for all the class B1 receptors bound to G proteins have been determined by cryo-EM in the past 5 years. Further advances in cryo-EM have uncovered dynamics of these receptors, ligands, and signaling partners. Here, we examine the recent structural underpinnings of the class B1 GPCRs with an emphasis on structure–function relationships. |
format | Online Article Text |
id | pubmed-10166269 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-101662692023-05-09 New Insights into the Structure and Function of Class B1 GPCRs Cary, Brian P Zhang, Xin Cao, Jianjun Johnson, Rachel M Piper, Sarah J Gerrard, Elliot J Wootten, Denise Sexton, Patrick M Endocr Rev Review G protein–coupled receptors (GPCRs) are the largest family of cell surface receptors. Class B1 GPCRs constitute a subfamily of 15 receptors that characteristically contain large extracellular domains (ECDs) and respond to long polypeptide hormones. Class B1 GPCRs are critical regulators of homeostasis, and, as such, many are important drug targets. While most transmembrane proteins, including GPCRs, are recalcitrant to crystallization, recent advances in cryo-electron microscopy (cryo-EM) have facilitated a rapid expansion of the structural understanding of membrane proteins. As a testament to this success, structures for all the class B1 receptors bound to G proteins have been determined by cryo-EM in the past 5 years. Further advances in cryo-EM have uncovered dynamics of these receptors, ligands, and signaling partners. Here, we examine the recent structural underpinnings of the class B1 GPCRs with an emphasis on structure–function relationships. Oxford University Press 2022-12-22 /pmc/articles/PMC10166269/ /pubmed/36546772 http://dx.doi.org/10.1210/endrev/bnac033 Text en © The Author(s) 2022. Published by Oxford University Press on behalf of the Endocrine Society. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs licence (https://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial reproduction and distribution of the work, in any medium, provided the original work is not altered or transformed in any way, and that the work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Review Cary, Brian P Zhang, Xin Cao, Jianjun Johnson, Rachel M Piper, Sarah J Gerrard, Elliot J Wootten, Denise Sexton, Patrick M New Insights into the Structure and Function of Class B1 GPCRs |
title | New Insights into the Structure and Function of Class B1 GPCRs |
title_full | New Insights into the Structure and Function of Class B1 GPCRs |
title_fullStr | New Insights into the Structure and Function of Class B1 GPCRs |
title_full_unstemmed | New Insights into the Structure and Function of Class B1 GPCRs |
title_short | New Insights into the Structure and Function of Class B1 GPCRs |
title_sort | new insights into the structure and function of class b1 gpcrs |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10166269/ https://www.ncbi.nlm.nih.gov/pubmed/36546772 http://dx.doi.org/10.1210/endrev/bnac033 |
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