Journal
TRENDS IN PHARMACOLOGICAL SCIENCES
Volume 35, Issue 1, Pages 12-22Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tips.2013.11.001
Keywords
class B G protein-coupled receptor (GPCR); glucagon receptor (GCGR); corticotropin-releasing factor receptor 1 (CRF1); crystal structure; ligand binding
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Funding
- PSI:Biology [U54 GM094618]
- Chinese Ministry of Health [2012ZX09304-011, 2013ZX09507002]
- Shanghai Science and Technology Development Fund [11DZ2292200]
- Novo Nordisk-Chinese Academy of Sciences Research Fund [NNCAS-2011-7]
- Thousand Talents Program in China
- European Cooperation in Science and Technology (COST) Action [CM1207]
- GPCR-Ligand Interactions, Structures, and Transmembrane Signalling: a European Research Network (GLISTEN)
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [U54GM094618] Funding Source: NIH RePORTER
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The secretin-like (class B) family of G protein-coupled receptors (GPCRs) are key players in hormonal homeostasis and are interesting drug targets for the treatment of several metabolic disorders (such as type 2 diabetes, osteoporosis, and obesity) and nervous system diseases (such as migraine, anxiety, and depression). The recently solved crystal structures of the transmembrane domains of the human glucagon receptor and human corticotropin-releasing factor receptor 1 have opened up new opportunities to study the structure and function of class B GPCRs. The current review shows how these structures offer more detailed explanations to previous biochemical and pharmacological studies of class B GPCRs, and provides new insights into their interactions with ligands.
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