2RH1

High resolution crystal structure of human B2-adrenergic G protein-coupled receptor.

Summary for 2RH1

• Entry DOI: 10.2210/pdb2rh1/pdb
• Related PRD ID: PRD_900001
• Descriptor: beta-2-adrenergic receptor/T4-lysozyme chimera, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, SULFATE ION, ... (10 entities in total)
• Functional Keywords: gpcr, 7tm, adrenergic, fusion, lipidic cubic phase, lipidic, mesophase, cholesterol, membrane protein, membrane protein - hydrolase complex, structural genomics, psi-2, protein structure initiative, accelerated technologies center for gene to 3d structure, atcg3d, gpcr network, membrane protein / hydrolase
• Biological source: Homo sapiens (human,); More
• Total number of polymer chains: 1
• Total formula weight: 60020.83

Authors

Cherezov, V.,Rosenbaum, D.M.,Hanson, M.A.,Rasmussen, S.G.F.,Thian, F.S.,Kobilka, T.S.,Choi, H.J.,Kuhn, P.,Weis, W.I.,Kobilka, B.K.,Stevens, R.C.,Accelerated Technologies Center for Gene to 3D Structure (ATCG3D),GPCR Network (GPCR) (deposition date: 2007-10-05, release date: 2007-10-30, Last modification date: 2024-10-30)

Primary citation

Cherezov, V.,Rosenbaum, D.M.,Hanson, M.A.,Rasmussen, S.G.,Thian, F.S.,Kobilka, T.S.,Choi, H.J.,Kuhn, P.,Weis, W.I.,Kobilka, B.K.,Stevens, R.C.
High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor.
Science, 318:1258-1265, 2007

PubMed Abstract: Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors constitute the largest family of eukaryotic signal transduction proteins that communicate across the membrane. We report the crystal structure of a human beta2-adrenergic receptor-T4 lysozyme fusion protein bound to the partial inverse agonist carazolol at 2.4 angstrom resolution. The structure provides a high-resolution view of a human G protein-coupled receptor bound to a diffusible ligand. Ligand-binding site accessibility is enabled by the second extracellular loop, which is held out of the binding cavity by a pair of closely spaced disulfide bridges and a short helical segment within the loop. Cholesterol, a necessary component for crystallization, mediates an intriguing parallel association of receptor molecules in the crystal lattice. Although the location of carazolol in the beta2-adrenergic receptor is very similar to that of retinal in rhodopsin, structural differences in the ligand-binding site and other regions highlight the challenges in using rhodopsin as a template model for this large receptor family.

PubMed: 17962520
DOI: 10.1126/science.1150577

Experimental method

X-RAY DIFFRACTION (2.4 Å)