5G53
Structure of the adenosine A2A receptor bound to an engineered G protein
Summary for 5G53
| Entry DOI | 10.2210/pdb5g53/pdb |
| Descriptor | ADENOSINE RECEPTOR A2A, ENGINEERED DOMAIN OF HUMAN G ALPHA S LONG ISOFORM, N-ETHYL-5'-CARBOXAMIDO ADENOSINE, ... (5 entities in total) |
| Functional Keywords | signaling protein, g protein coupled receptor, adenosine receptor, seven-helix receptor, integral membrane protein, gpcr, engineered g protein, gpcr-g protein complex, mini-gs |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Total number of polymer chains | 4 |
| Total formula weight | 124745.90 |
| Authors | Carpenter, B.,Nehme, R.,Warne, T.,Leslie, A.G.W.,Tate, C.G. (deposition date: 2016-05-19, release date: 2016-08-03, Last modification date: 2024-11-13) |
| Primary citation | Carpenter, B.,Nehme, R.,Warne, T.,Leslie, A.G.W.,Tate, C.G. Structure of the Adenosine A2A Receptor Bound to an Engineered G Protein Nature, 536:104-, 2016 Cited by PubMed Abstract: G-protein-coupled receptors (GPCRs) are essential components of the signalling network throughout the body. To understand the molecular mechanism of G-protein-mediated signalling, solved structures of receptors in inactive conformations and in the active conformation coupled to a G protein are necessary. Here we present the structure of the adenosine A(2A) receptor (A(2A)R) bound to an engineered G protein, mini-Gs, at 3.4 Å resolution. Mini-Gs binds to A(2A)R through an extensive interface (1,048 Å2) that is similar, but not identical, to the interface between Gs and the β2-adrenergic receptor. The transition of the receptor from an agonist-bound active-intermediate state to an active G-protein-bound state is characterized by a 14 Å shift of the cytoplasmic end of transmembrane helix 6 (H6) away from the receptor core, slight changes in the positions of the cytoplasmic ends of H5 and H7 and rotamer changes of the amino acid side chains Arg3.50, Tyr5.58 and Tyr7.53. There are no substantial differences in the extracellular half of the receptor around the ligand binding pocket. The A(2A)R-mini-Gs structure highlights both the diversity and similarity in G-protein coupling to GPCRs and hints at the potential complexity of the molecular basis for G-protein specificity. PubMed: 27462812DOI: 10.1038/NATURE18966 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
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