The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.
Structure of the Adenosine A2A Receptor in Complex with ZM241385 and the Xanthines XAC and Caffeine
Open accessAbstract
SUMMARY Methylxanthines, including caffeine and theophylline are among the most widely consumed stimulant drugs in the world. These effects are mediated primarily via blockade of adenosine receptors. Xanthine analogues with improved properties have been developed as potential treatments for diseases such as Parkinson’s disease. Here we report the structures of a thermostabilised adenosine A2A receptor in complex with the xanthines xanthine amine congener and caffeine, as well as the A2A selective inverse agonist ZM241385. The receptor is crystallised in the inactive state conformation as defined by the presence of a salt bridge known as the ionic lock. The complete third intracellular loop, responsible for G protein coupling, is visible consisting of extended helices 5 and 6. The structures provide new insight into the features which define the ligand binding pocket of the adenosine receptor for ligands of diverse chemotypes as well as the cytoplasmic regions which interact with signal transduction proteins.
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Citations
Cites
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
The CCP4 suite: programs for protein crystallography
Collaborative Computational Project, N. 4. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,270
PHENIX: a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2012) · International Tables for Crystallography · doi:10.1107/97809553602060000865 · Cited by 7,334
G PROTEINS: TRANSDUCERS OF RECEPTOR-GENERATED SIGNALS
Gilman, A. G. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.003151 · Cited by 6,381
LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions
Wallace, A. C., Laskowski, R. A., & Thornton, J. M. (1995) · "Protein Engineering, Design and Selection" · doi:10.1093/protein/8.2.127 · Cited by 5,690
Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor
Palczewski, K., Kumasaka, T., Hori, T., Behnke, C. A., Motoshima, H., Fox, B. A., Trong, I. L., Teller, D. C., Okada, T., Stenkamp, R. E., et al. (2000) · Science · doi:10.1126/science.289.5480.739 · Cited by 5,637
Scaling and assessment of data quality
Evans, P. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444905036693 · Cited by 4,374
High-Resolution Crystal Structure of an Engineered Human β 2 -Adrenergic G Protein–Coupled Receptor
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., et al. (2007) · Science · doi:10.1126/science.1150577 · Cited by 3,264
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Molecular signatures of G-protein-coupled receptors
Venkatakrishnan, A. J., Deupi, X., Lebon, G., Tate, C. G., Schertler, G. F., & Babu, M. M. (2013) · Nature · doi:10.1038/nature11896 · Cited by 1,497
Self-citationMicrobial and Animal Rhodopsins: Structures, Functions, and Molecular Mechanisms
Ernst, O. P., Lodowski, D. T., Elstner, M., Hegemann, P., Brown, L. S., & Kandori, H. (2014) · Chemical Reviews · doi:10.1021/cr4003769 · Cited by 1,153
The Current State of Peptide Drug Discovery: Back to the Future?
Henninot, A., Collins, J. C., & Nuss, J. M. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00318 · Cited by 1,113
Caffeine: Cognitive and Physical Performance Enhancer or Psychoactive Drug?
Cappelletti, S., Daria, P., Sani, G., & Aromatario, M. (2015) · Current Neuropharmacology · doi:10.2174/1570159x13666141210215655 · Cited by 631
“Recent experimental evidence suggests that the primary target of the neuroprotective effects of caffeine [124, 125] is either the activation or the inhibition of the A1 and A2A adenosine receptor subtypes [126, 127] (Table 1; findings not discussed in this review).”
BackgroundStructure of the nociceptin/orphanin FQ receptor in complex with a peptide mimetic
Thompson, A. A., Liu, W., Chun, E., Katritch, V., Wu, H., Vardy, E., Huang, X.-P., Trapella, C., Guerrini, R., Calo, G., et al. (2012) · Nature · doi:10.1038/nature11085 · Cited by 477
Metadata
- Authors
- Doré, A. S., Robertson, N., Errey, J. C., Ng, I., Hollenstein, K., Tehan, B., Hurrell, E., Bennett, K., Congreve, M., Magnani, F., Tate, C. G., Weir, M., & Marshall, F. H.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2011-09
- Volume
- 19
- Issue
- 9
- Pages
- 1283-1293
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W2142322475
- Cited by
- 553
- References
- 50
- FWCI
- 19.28
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Doré, A. S., Robertson, N., Errey, J. C., Ng, I., Hollenstein, K., Tehan, B., Hurrell, E., Bennett, K., Congreve, M., Magnani, F., Tate, C. G., Weir, M., & Marshall, F. H. (2011). Structure of the Adenosine A2A Receptor in Complex with ZM241385 and the Xanthines XAC and Caffeine. Structure. https://doi.org/10.1016/j.str.2011.06.014
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