Recent advances in the determination of G protein-coupled receptor structures

Research output: Contribution to journalArticleResearchpeer-review

Abstract

G protein-coupled receptors (GPCRs) are the largest superfamily of cell surface receptor proteins and are important drug targets for many human diseases. In the last decade, remarkable progress has been made in the determination of atomic structures of GPCRs with over 200 structures from 53 unique receptors having been solved. Technological advances in protein engineering and X-ray crystallography have driven much of the progress to date. However, recent advances in cryo-electron microscopy have facilitated the structural determination of three new structures of active-state GPCRs in complex with heterotrimeric G protein. These advances have led to significant breakthroughs in our understanding of GPCR biology including not only how signal transducers such as G proteins or arrestins interact with receptors, but also pave the way for future structure-based drug design.

Original languageEnglish
Pages (from-to)28-34
Number of pages7
JournalCurrent Opinion in Structural Biology
Volume51
DOIs
Publication statusPublished - 1 Aug 2018

Cite this

@article{c647241bac9543e5992f3948062d666c,
title = "Recent advances in the determination of G protein-coupled receptor structures",
abstract = "G protein-coupled receptors (GPCRs) are the largest superfamily of cell surface receptor proteins and are important drug targets for many human diseases. In the last decade, remarkable progress has been made in the determination of atomic structures of GPCRs with over 200 structures from 53 unique receptors having been solved. Technological advances in protein engineering and X-ray crystallography have driven much of the progress to date. However, recent advances in cryo-electron microscopy have facilitated the structural determination of three new structures of active-state GPCRs in complex with heterotrimeric G protein. These advances have led to significant breakthroughs in our understanding of GPCR biology including not only how signal transducers such as G proteins or arrestins interact with receptors, but also pave the way for future structure-based drug design.",
author = "Thal, {David M} and Ziva Vuckovic and Draper-Joyce, {Christopher J} and Yi-Lynn Liang and Alisa Glukhova and Arthur Christopoulos and Sexton, {Patrick M}",
year = "2018",
month = "8",
day = "1",
doi = "10.1016/j.sbi.2018.03.002",
language = "English",
volume = "51",
pages = "28--34",
journal = "Current Opinion in Structural Biology",
issn = "0959-440X",
publisher = "Elsevier",

}

TY - JOUR

T1 - Recent advances in the determination of G protein-coupled receptor structures

AU - Thal, David M

AU - Vuckovic, Ziva

AU - Draper-Joyce, Christopher J

AU - Liang, Yi-Lynn

AU - Glukhova, Alisa

AU - Christopoulos, Arthur

AU - Sexton, Patrick M

PY - 2018/8/1

Y1 - 2018/8/1

N2 - G protein-coupled receptors (GPCRs) are the largest superfamily of cell surface receptor proteins and are important drug targets for many human diseases. In the last decade, remarkable progress has been made in the determination of atomic structures of GPCRs with over 200 structures from 53 unique receptors having been solved. Technological advances in protein engineering and X-ray crystallography have driven much of the progress to date. However, recent advances in cryo-electron microscopy have facilitated the structural determination of three new structures of active-state GPCRs in complex with heterotrimeric G protein. These advances have led to significant breakthroughs in our understanding of GPCR biology including not only how signal transducers such as G proteins or arrestins interact with receptors, but also pave the way for future structure-based drug design.

AB - G protein-coupled receptors (GPCRs) are the largest superfamily of cell surface receptor proteins and are important drug targets for many human diseases. In the last decade, remarkable progress has been made in the determination of atomic structures of GPCRs with over 200 structures from 53 unique receptors having been solved. Technological advances in protein engineering and X-ray crystallography have driven much of the progress to date. However, recent advances in cryo-electron microscopy have facilitated the structural determination of three new structures of active-state GPCRs in complex with heterotrimeric G protein. These advances have led to significant breakthroughs in our understanding of GPCR biology including not only how signal transducers such as G proteins or arrestins interact with receptors, but also pave the way for future structure-based drug design.

UR - http://www.scopus.com/inward/record.url?scp=85045734753&partnerID=8YFLogxK

U2 - 10.1016/j.sbi.2018.03.002

DO - 10.1016/j.sbi.2018.03.002

M3 - Article

VL - 51

SP - 28

EP - 34

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

SN - 0959-440X

ER -