6H7O
ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND WEAK PARTIAL AGONIST CYANOPINDOLOL AND NANOBODY Nb6B9
Summary for 6H7O
| Entry DOI | 10.2210/pdb6h7o/pdb |
| Descriptor | Thioredoxin 1, Beta-1 adrenergic receptor, Camelid antibody fragment Nb6B9, ... (7 entities in total) |
| Functional Keywords | beta1 adrenoceptor, activated, weak partial agonist, nanobody, electron transport |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 6 |
| Total formula weight | 122924.32 |
| Authors | Warne, T.,Edwards, P.C.,Dore, A.S.,Leslie, A.G.W.,Tate, C.G. (deposition date: 2018-07-31, release date: 2018-10-17, Last modification date: 2024-01-17) |
| Primary citation | Warne, T.,Edwards, P.C.,Dore, A.S.,Leslie, A.G.W.,Tate, C.G. Molecular basis for high-affinity agonist binding in GPCRs. Science, 364:775-778, 2019 Cited by PubMed Abstract: G protein-coupled receptors (GPCRs) in the G protein-coupled active state have higher affinity for agonists as compared with when they are in the inactive state, but the molecular basis for this is unclear. We have determined four active-state structures of the β-adrenoceptor (βAR) bound to conformation-specific nanobodies in the presence of agonists of varying efficacy. Comparison with inactive-state structures of βAR bound to the identical ligands showed a 24 to 42% reduction in the volume of the orthosteric binding site. Potential hydrogen bonds were also shorter, and there was up to a 30% increase in the number of atomic contacts between the receptor and ligand. This explains the increase in agonist affinity of GPCRs in the active state for a wide range of structurally distinct agonists. PubMed: 31072904DOI: 10.1126/science.aau5595 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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