3QAK

Agonist bound structure of the human adenosine A2a receptor

Summary for 3QAK

• Entry DOI: 10.2210/pdb3qak/pdb
• Related: 3eml
• Descriptor: Adenosine receptor A2a,lysozyme chimera, 6-(2,2-diphenylethylamino)-9-[(2R,3R,4S,5S)-5-(ethylcarbamoyl)-3,4-dihydroxy-oxolan-2-yl]-N-[2-[(1-pyridin-2-ylpiperidin-4-yl)carbamoylamino]ethyl]purine-2-carboxamide, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (4 entities in total)
• Functional Keywords: structural genomics, protein structure initiative, joint center for innovative membrane protein technologies, jcimpt, membrane protein, receptor, gpcr network, gpcr, signaling protein, hydrolase, psi-biology
• Biological source: Homo Sapien; More
• Cellular location: Cell membrane; Multi-pass membrane protein: P29274
• Total number of polymer chains: 1
• Total formula weight: 56230.72

Authors

Xu, F.,Wu, H.,Katritch, V.,Han, G.W.,Cherezov, V.,Stevens, R.,GPCR Network (GPCR) (deposition date: 2011-01-11, release date: 2011-03-09, Last modification date: 2024-10-09)

Primary citation

Xu, F.,Wu, H.,Katritch, V.,Han, G.W.,Jacobson, K.A.,Gao, Z.G.,Cherezov, V.,Stevens, R.C.
Structure of an agonist-bound human A2A adenosine receptor.
Science, 332:322-327, 2011

PubMed Abstract: Activation of G protein-coupled receptors upon agonist binding is a critical step in the signaling cascade for this family of cell surface proteins. We report the crystal structure of the A(2A) adenosine receptor (A(2A)AR) bound to an agonist UK-432097 at 2.7 angstrom resolution. Relative to inactive, antagonist-bound A(2A)AR, the agonist-bound structure displays an outward tilt and rotation of the cytoplasmic half of helix VI, a movement of helix V, and an axial shift of helix III, resembling the changes associated with the active-state opsin structure. Additionally, a seesaw movement of helix VII and a shift of extracellular loop 3 are likely specific to A(2A)AR and its ligand. The results define the molecule UK-432097 as a "conformationally selective agonist" capable of receptor stabilization in a specific active-state configuration.

PubMed: 21393508
DOI: 10.1126/science.1202793

Experimental method

X-RAY DIFFRACTION (2.71 Å)