Journal
NATURE
Volume 494, Issue 7436, Pages 185-194Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature11896
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Funding
- UK Medical Research Council [U105185859, U105197215]
- HFSP [RGY0073/2010]
- EMBO Young Investigator Program
- ERASysBio+ (GRAPPLE)
- LMB Cambridge Scholarship
- St. John's College Benefactor Scholarship
- Heptares Therapeutics
- CNRS
- Agence Nationale de la Recherche [ANR-09-BLAN-0272]
- Swiss National Science Foundation [31003A_132815]
- ETH Zurich within the framework of the National Center for Competence in Research in Structural Biology Program
- Medical Research Council Technology Development Gap Fund
- Pfizer
- MRC [MC_U105197215, MC_U105185859] Funding Source: UKRI
- Swiss National Science Foundation (SNF) [31003A_132815] Funding Source: Swiss National Science Foundation (SNF)
- Medical Research Council [MC_U105197215, MC_U105185859] Funding Source: researchfish
- Agence Nationale de la Recherche (ANR) [ANR-09-BLAN-0272] Funding Source: Agence Nationale de la Recherche (ANR)
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G-protein-coupled receptors (GPCRs) are physiologically important membrane proteins that sense signalling molecules such as hormones and neurotransmitters, and are the targets of several prescribed drugs. Recent exciting developments are providing unprecedented insights into the structure and function of several medically important GPCRs. Here, through a systematic analysis of high-resolution GPCR structures, we uncover a conserved network of non-covalent contacts that defines the GPCR fold. Furthermore, our comparative analysis reveals characteristic features of ligand binding and conformational changes during receptor activation. A holistic understanding that integrates molecular and systems biology of GPCRs holds promise for new therapeutics and personalized medicine.
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