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Structure of an Agonist-Bound Human A2A Adenosine Receptor

Structure of an Agonist-Bound Human A2A Adenosine Receptor

Fei Xu, Huixian Wu, Vsevolod Katritch, Gye Won Han, Kenneth A Jacobson, Zhan-Guo Gao, Vadim Cherezov, Raymond C Stevens

Science. 2011 Apr 15;332(6027):322-7.

PMID: 21393508

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP380221636	UK-432097		380221-63-6	Price

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