2R4S

Crystal structure of the human beta2 adrenoceptor

2R4S の概要

• エントリーDOI: 10.2210/pdb2r4s/pdb
• 関連するPDBエントリー: 2R4R
• 分子名称: Beta-2 adrenergic receptor, antibody for beta2 adrenoceptor, light chain, antibody for beta2 adrenoceptor, heavy chain (3 entities in total)
• 機能のキーワード: transmembrane helix, g-protein coupled receptor, glycoprotein, lipoprotein, palmitate, phosphorylation, receptor, transducer, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell membrane ; Multi- pass membrane protein : P07550
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 86045.80

構造登録者

Rasmussen, S.G.F.,Choi, H.J.,Rosenbaum, D.M.,Kobilka, T.S.,Thian, F.S.,Edwards, P.C.,Burghammer, M.,Ratnala, V.R.,Sanishvili, R.,Fischetti, R.F.,Schertler, G.F.,Weis, W.I.,Kobilka, B.K. (登録日: 2007-08-31, 公開日: 2007-11-06, 最終更新日: 2024-10-16)

主引用文献

Rasmussen, S.G.F.,Choi, H.J.,Rosenbaum, D.M.,Kobilka, T.S.,Thian, F.S.,Edwards, P.C.,Burghammer, M.,Ratnala, V.R.,Sanishvili, R.,Fischetti, R.F.,Schertler, G.F.,Weis, W.I.,Kobilka, B.K.
Crystal structure of the human beta2 adrenergic G-protein-coupled receptor.
Nature, 450:383-387, 2007

PubMed Abstract: Structural analysis of G-protein-coupled receptors (GPCRs) for hormones and neurotransmitters has been hindered by their low natural abundance, inherent structural flexibility, and instability in detergent solutions. Here we report a structure of the human beta2 adrenoceptor (beta2AR), which was crystallized in a lipid environment when bound to an inverse agonist and in complex with a Fab that binds to the third intracellular loop. Diffraction data were obtained by high-brilliance microcrystallography and the structure determined at 3.4 A/3.7 A resolution. The cytoplasmic ends of the beta2AR transmembrane segments and the connecting loops are well resolved, whereas the extracellular regions of the beta2AR are not seen. The beta2AR structure differs from rhodopsin in having weaker interactions between the cytoplasmic ends of transmembrane (TM)3 and TM6, involving the conserved E/DRY sequences. These differences may be responsible for the relatively high basal activity and structural instability of the beta2AR, and contribute to the challenges in obtaining diffraction-quality crystals of non-rhodopsin GPCRs.

PubMed: 17952055
DOI: 10.1038/nature06325

実験手法

X-RAY DIFFRACTION (3.4 Å)