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7XK8

Cryo-EM structure of the Neuromedin U receptor 2 (NMUR2) in complex with G Protein and its endogeneous Peptide-Agonist NMU25

Summary for 7XK8
Entry DOI10.2210/pdb7xk8/pdb
EMDB information33247
DescriptorNeuromedin-U-25, Neuromedin-U receptor 2, Guanine nucleotide-binding protein G(i) subunit alpha-1, ... (5 entities in total)
Functional Keywordsgpcr, complex, membrane protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains5
Total formula weight134838.01
Authors
Zhao, W.,Wenru, Z.,Mu, W.,Minmin, L.,Shutian, C.,Tingting, T.,Gisela, S.,Holger, W.,Albert, B.,Cuiying, Y.,Xiaojing, C.,Han, S.,Wu, B.,Zhao, Q. (deposition date: 2022-04-19, release date: 2023-02-22, Last modification date: 2024-11-13)
Primary citationZhao, W.,Zhang, W.,Wang, M.,Lu, M.,Chen, S.,Tang, T.,Schnapp, G.,Wagner, H.,Brennauer, A.,Yi, C.,Chu, X.,Han, S.,Wu, B.,Zhao, Q.
Ligand recognition and activation of neuromedin U receptor 2.
Nat Commun, 13:7955-7955, 2022
Cited by
PubMed Abstract: Neuromedin U receptor 2 (NMU2), an emerging attractive target for treating obesity, has shown the capability in reducing food intake and regulating energy metabolism when activated. However, drug development of NMU2 was deferred partially due to the lack of structural information. Here, we present the cryo-electron microscopy (cryo-EM) structure of NMU2 bound to the endogenous agonist NmU-25 and G at 3.3 Å resolution. Combined with functional and computational data, the structure reveals the key factors that govern the recognition and selectivity of peptide agonist as well as non-peptide antagonist, providing the structural basis for design of novel and highly selective drugs targeting NMU2. In addition, a 25-degree rotation of G protein in reference to NMU2 is also observed compared in other structures of class A GPCR-G complexes, suggesting heterogeneity in the processes of G protein-coupled receptors (GPCRs) activation and G protein coupling.
PubMed: 36575163
DOI: 10.1038/s41467-022-34814-4
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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