7DDZ
The Crystal Structure of Human Neuropeptide Y Y2 Receptor with JNJ-31020028
Summary for 7DDZ
| Entry DOI | 10.2210/pdb7ddz/pdb |
| Descriptor | Human Neuropeptide Y Y2 Receptor fusion protein, ~{N}-[4-[4-[(1~{S})-2-(diethylamino)-2-oxidanylidene-1-phenyl-ethyl]piperazin-1-yl]-3-fluoranyl-phenyl]-2-pyridin-3-yl-benzamide, FLAVIN MONONUCLEOTIDE (3 entities in total) |
| Functional Keywords | neuropeptide y y2 receptor, membrane protein |
| Biological source | Enterobacteria phage RB59 More |
| Total number of polymer chains | 1 |
| Total formula weight | 75307.32 |
| Authors | |
| Primary citation | Tang, T.,Hartig, C.,Chen, Q.,Zhao, W.,Kaiser, A.,Zhang, X.,Zhang, H.,Qu, H.,Yi, C.,Ma, L.,Han, S.,Zhao, Q.,Beck-Sickinger, A.G.,Wu, B. Structural basis for ligand recognition of the neuropeptide Y Y 2 receptor. Nat Commun, 12:737-737, 2021 Cited by PubMed Abstract: The human neuropeptide Y (NPY) Y receptor (YR) plays essential roles in food intake, bone formation and mood regulation, and has been considered an important drug target for obesity and anxiety. However, development of drugs targeting YR remains challenging with no success in clinical application yet. Here, we report the crystal structure of YR bound to a selective antagonist JNJ-31020028 at 2.8 Å resolution. The structure reveals molecular details of the ligand-binding mode of YR. Combined with mutagenesis studies, the YR structure provides insights into key factors that define antagonistic activity of diverse antagonists. Comparison with the previously determined antagonist-bound YR structures identified receptor-ligand interactions that play different roles in modulating receptor activation and mediating ligand selectivity. These findings deepen our understanding about molecular mechanisms of ligand recognition and subtype specificity of NPY receptors, and would enable structure-based drug design. PubMed: 33531491DOI: 10.1038/s41467-021-21030-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
Download full validation report
