7XBD
Cryo-EM structure of human galanin receptor 2
Summary for 7XBD
| Entry DOI | 10.2210/pdb7xbd/pdb |
| EMDB information | 33103 |
| Descriptor | Galanin receptor type 2, Guanine nucleotide-binding protein G(q) subunit alpha, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, ... (6 entities in total) |
| Functional Keywords | gpcr, membrane protein, galanin |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 145743.01 |
| Authors | Ishimoto, N.,Kita, S.,Park, S.Y. (deposition date: 2022-03-21, release date: 2022-07-13, Last modification date: 2024-11-06) |
| Primary citation | Heo, Y.,Ishimoto, N.,Jeon, Y.E.,Yun, J.H.,Ohki, M.,Anraku, Y.,Sasaki, M.,Kita, S.,Fukuhara, H.,Ikuta, T.,Kawakami, K.,Inoue, A.,Maenaka, K.,Tame, J.R.H.,Lee, W.,Park, S.Y. Structure of the human galanin receptor 2 bound to galanin and Gq reveals the basis of ligand specificity and how binding affects the G-protein interface. Plos Biol., 20:e3001714-e3001714, 2022 Cited by PubMed Abstract: Galanin is a neuropeptide expressed in the central and peripheral nervous systems, where it regulates various processes including neuroendocrine release, cognition, and nerve regeneration. Three G-protein coupled receptors (GPCRs) for galanin have been discovered, which is the focus of efforts to treat diseases including Alzheimer's disease, anxiety, and addiction. To understand the basis of the ligand preferences of the receptors and to assist structure-based drug design, we used cryo-electron microscopy (cryo-EM) to solve the molecular structure of GALR2 bound to galanin and a cognate heterotrimeric G-protein, providing a molecular view of the neuropeptide binding site. Mutant proteins were assayed to help reveal the basis of ligand specificity, and structural comparison between the activated GALR2 and inactive hβ2AR was used to relate galanin binding to the movements of transmembrane (TM) helices and the G-protein interface. PubMed: 35913979DOI: 10.1371/journal.pbio.3001714 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.11 Å) |
Structure validation
Download full validation report
