5VBL
Structure of apelin receptor in complex with agonist peptide
Summary for 5VBL
| Entry DOI | 10.2210/pdb5vbl/pdb |
| Descriptor | agonist peptide, Apelin receptor,Rubredoxin,Apelin receptor Chimera, ZINC ION, ... (5 entities in total) |
| Functional Keywords | human apelin receptor complex, agonist peptide, amg3054, gpcr, rubredoxin, membrane protein, lcp, synchrotron radiation, peptide-gcpr recognition, cardiovascular drug target, specific recognition, binding specificity, designed agonist peptide mimic, isopeptide |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Cell membrane : P35414 |
| Total number of polymer chains | 2 |
| Total formula weight | 49248.92 |
| Authors | Ma, Y.,Yue, Y.,Ma, Y.,Zhang, Q.,Zhou, Q.,Song, Y.,Shen, Y.,Li, X.,Ma, X.,Li, C.,Hanson, M.A.,Han, G.W.,Sickmier, E.A.,Swaminath, G.,Zhao, S.,Stevems, R.C.,Hu, L.A.,Zhong, W.,Zhang, M.,Xu, F. (deposition date: 2017-03-29, release date: 2017-05-31, Last modification date: 2023-11-15) |
| Primary citation | Ma, Y.,Yue, Y.,Ma, Y.,Zhang, Q.,Zhou, Q.,Song, Y.,Shen, Y.,Li, X.,Ma, X.,Li, C.,Hanson, M.A.,Han, G.W.,Sickmier, E.A.,Swaminath, G.,Zhao, S.,Stevens, R.C.,Hu, L.A.,Zhong, W.,Zhang, M.,Xu, F. Structural Basis for Apelin Control of the Human Apelin Receptor Structure, 25:858-866.e4, 2017 Cited by PubMed Abstract: Apelin receptor (APJR) is a key regulator of human cardiovascular function and is activated by two different endogenous peptide ligands, apelin and Elabela, each with different isoforms diversified by length and amino acid sequence. Here we report the 2.6-Å resolution crystal structure of human APJR in complex with a designed 17-amino-acid apelin mimetic peptide agonist. The structure reveals that the peptide agonist adopts a lactam constrained curved two-site ligand binding mode. Combined with mutation analysis and molecular dynamics simulations with apelin-13 binding to the wild-type APJR, this structure provides a mechanistic understanding of apelin recognition and binding specificity. Comparison of this structure with that of other peptide receptors suggests that endogenous peptide ligands with a high degree of conformational flexibility may bind and modulate the receptors via a similar two-site binding mechanism. PubMed: 28528775DOI: 10.1016/j.str.2017.04.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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