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Crystal structure of glucagon receptor (GCGR)

A crystal structure of GCGR could help drug discovery efforts targeting class B GPCRs. Researchers solved the structure of the 7-transmembrane helical domain of GCGR at 3.4 Å resolution. The structure showed that a stalk extends from the N terminus of helix I that may be involved in glucagon (GCG) binding. Compared with class A GPCR structures, GCGR has a large ligand-binding pocket. Next steps could include building models of interactions between peptide ligands and other class B GPCRs.

SciBX 6(33); doi:10.1038/scibx.2013.911
Published online Aug. 29, 2013

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Siu, F.Y. et al. Nature; published online
July 17, 2013;
doi:10.1038/nature12393
Contact: Raymond C. Stevens, The Scripps Research Institute, La Jolla, Calif.
e-mail:

stevens@scripps.edu
Contact: Ming-Wei Wang, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China
e-mail:

wangmw@mail.shcnc.ac.cn