3EML

The 2.6 A Crystal Structure of a Human A2A Adenosine Receptor bound to ZM241385.

3EML の概要

• エントリーDOI: 10.2210/pdb3eml/pdb
• 分子名称: Human Adenosine A2A receptor/T4 lysozyme chimera, 4-{2-[(7-amino-2-furan-2-yl[1,2,4]triazolo[1,5-a][1,3,5]triazin-5-yl)amino]ethyl}phenol, STEARIC ACID, ... (5 entities in total)
• 機能のキーワード: adenosine, caffeine, gpcr, membrane protein, receptor, lcp, mesophase, structural genomics, psi-2, protein structure initiative, accelerated technologies center for gene to 3d structure, atcg3d, gpcr network
• 由来する生物種: Homo sapiens; 詳細
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P29274
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57171.93

構造登録者

Jaakola, V.-P.,Griffith, M.T.,Hanson, M.A.,Cherezov, V.,Chien, E.Y.T.,Lane, J.R.,Ijzerman, A.P.,Stevens, R.C.,Accelerated Technologies Center for Gene to 3D Structure (ATCG3D),GPCR Network (GPCR) (登録日: 2008-09-24, 公開日: 2008-10-14, 最終更新日: 2024-10-30)

主引用文献

Jaakola, V.P.,Griffith, M.T.,Hanson, M.A.,Cherezov, V.,Chien, E.Y.,Lane, J.R.,Ijzerman, A.P.,Stevens, R.C.
The 2.6 Angstrom Crystal Structure of a Human A2A Adenosine Receptor Bound to an Antagonist.
Science, 322:1211-1217, 2008

PubMed Abstract: The adenosine class of heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) mediates the important role of extracellular adenosine in many physiological processes and is antagonized by caffeine. We have determined the crystal structure of the human A2A adenosine receptor, in complex with a high-affinity subtype-selective antagonist, ZM241385, to 2.6 angstrom resolution. Four disulfide bridges in the extracellular domain, combined with a subtle repacking of the transmembrane helices relative to the adrenergic and rhodopsin receptor structures, define a pocket distinct from that of other structurally determined GPCRs. The arrangement allows for the binding of the antagonist in an extended conformation, perpendicular to the membrane plane. The binding site highlights an integral role for the extracellular loops, together with the helical core, in ligand recognition by this class of GPCRs and suggests a role for ZM241385 in restricting the movement of a tryptophan residue important in the activation mechanism of the class A receptors.

PubMed: 18832607
DOI: 10.1126/science.1164772

実験手法

X-RAY DIFFRACTION (2.6 Å)