G protein-coupled receptors: the evolution of structural insight
G protein-coupled receptors (GPCR) comprise a diverse superfamily of over 800 proteins that have gained relevance as biological targets for pharmaceutical drug design. Although these receptors have been investigated for decades, three-dimensional structures of GPCR have only recently become availabl...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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AIMS Press
2017-08-01
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| Series: | AIMS Biophysics |
| Subjects: | |
| Online Access: | http://www.aimspress.com/biophysics/article/1574/fulltext.html |
| _version_ | 1811343010705702912 |
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| author | Samantha B. Gacasan Daniel L. Baker Abby L. Parrill |
| author_facet | Samantha B. Gacasan Daniel L. Baker Abby L. Parrill |
| author_sort | Samantha B. Gacasan |
| collection | DOAJ |
| description | G protein-coupled receptors (GPCR) comprise a diverse superfamily of over 800 proteins that have gained relevance as biological targets for pharmaceutical drug design. Although these receptors have been investigated for decades, three-dimensional structures of GPCR have only recently become available. In this review, we focus on the technological advancements that have facilitated efforts to gain insights into GPCR structure. Progress in these efforts began with the initial crystal structure determination of rhodopsin (PDB: 1F88) in 2000 and has continued to the most recently published structure of the A<sub>1A</sub>R (PDB: 5UEN) in 2017. Numerous experimental developments over the past two decades have opened the door for widespread GPCR structural characterization. These efforts have resulted in the determination of three-dimensional structures for over 40 individual GPCR family members. Herein we present a comprehensive list and comparative analysis of over 180 individual GPCR structures. This includes a summary of different GPCR functional states crystallized with agonists, dual agonists, partial agonists, inverse agonists, antagonists, and allosteric modulators. |
| first_indexed | 2024-04-13T19:22:14Z |
| format | Article |
| id | doaj.art-2b337bf9c3b845a5bb723a1d1dd304b5 |
| institution | Directory Open Access Journal |
| issn | 2377-9098 |
| language | English |
| last_indexed | 2024-04-13T19:22:14Z |
| publishDate | 2017-08-01 |
| publisher | AIMS Press |
| record_format | Article |
| series | AIMS Biophysics |
| spelling | doaj.art-2b337bf9c3b845a5bb723a1d1dd304b52022-12-22T02:33:29ZengAIMS PressAIMS Biophysics2377-90982017-08-014349152710.3934/biophy.2017.3.491biophys-04-00491G protein-coupled receptors: the evolution of structural insightSamantha B. Gacasan0Daniel L. Baker1Abby L. Parrill2Department of Chemistry, University of Memphis, 3744 Walker Ave, Memphis, TN 38152, USADepartment of Chemistry, University of Memphis, 3744 Walker Ave, Memphis, TN 38152, USADepartment of Chemistry, University of Memphis, 3744 Walker Ave, Memphis, TN 38152, USAG protein-coupled receptors (GPCR) comprise a diverse superfamily of over 800 proteins that have gained relevance as biological targets for pharmaceutical drug design. Although these receptors have been investigated for decades, three-dimensional structures of GPCR have only recently become available. In this review, we focus on the technological advancements that have facilitated efforts to gain insights into GPCR structure. Progress in these efforts began with the initial crystal structure determination of rhodopsin (PDB: 1F88) in 2000 and has continued to the most recently published structure of the A<sub>1A</sub>R (PDB: 5UEN) in 2017. Numerous experimental developments over the past two decades have opened the door for widespread GPCR structural characterization. These efforts have resulted in the determination of three-dimensional structures for over 40 individual GPCR family members. Herein we present a comprehensive list and comparative analysis of over 180 individual GPCR structures. This includes a summary of different GPCR functional states crystallized with agonists, dual agonists, partial agonists, inverse agonists, antagonists, and allosteric modulators.http://www.aimspress.com/biophysics/article/1574/fulltext.htmlG protein-coupled receptorsfusion proteinsx-ray crystallographyligand bindingagonistsantagonistsinverse agonistsallosteric modulatorsextracellular loopsintracellular loops7TM domain |
| spellingShingle | Samantha B. Gacasan Daniel L. Baker Abby L. Parrill G protein-coupled receptors: the evolution of structural insight AIMS Biophysics G protein-coupled receptors fusion proteins x-ray crystallography ligand binding agonists antagonists inverse agonists allosteric modulators extracellular loops intracellular loops 7TM domain |
| title | G protein-coupled receptors: the evolution of structural insight |
| title_full | G protein-coupled receptors: the evolution of structural insight |
| title_fullStr | G protein-coupled receptors: the evolution of structural insight |
| title_full_unstemmed | G protein-coupled receptors: the evolution of structural insight |
| title_short | G protein-coupled receptors: the evolution of structural insight |
| title_sort | g protein coupled receptors the evolution of structural insight |
| topic | G protein-coupled receptors fusion proteins x-ray crystallography ligand binding agonists antagonists inverse agonists allosteric modulators extracellular loops intracellular loops 7TM domain |
| url | http://www.aimspress.com/biophysics/article/1574/fulltext.html |
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