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Beyond Rhodopsin: G Protein-Coupled Receptor Structure and Modeling Incorporating the β2-adrenergic and Adenosine A2A Crystal Structures

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Chemoinformatics and Computational Chemical Biology

Part of the book series: Methods in Molecular Biology ((MIMB,volume 672))

Abstract

For quite some time, the majority of GPCR models have been based on a single template structure: dark-adapted bovine rhodopsin. The recent solution of β2AR, β1AR and adenosine A2A receptor crystal structures has dramatically expanded the GPCR structural landscape and provided many new insights into receptor conformation and ligand binding. They will serve as templates for the next generation of GPCR models, but also allow direct validation of previous models and computational techniques. This review summarizes key findings from the new structures, comparison of existing models to these structures and highlights new models constructed from these templates.

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Acknowledgments

The authors would like to thank Dr. Roy Kimura for providing the program to generate the snake plot in Fig. 1 and Dr. Stan Krystek for his input and critical reading of the manuscript.

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  1. Computer Aided Drug Design, Pharmaceutical Research Institute, Bristol-Myers Squibb Company, Princeton, NJ, USA

    Andrew J. Tebben & Dora M. Schnur

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  1. , Department of Life Science Informatics, Rheinische Friedrich-Wilhelms-Universitä, Dahlmannstr. 2, Bonn, 53113, Germany

    Jürgen Bajorath

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Tebben, A.J., Schnur, D.M. (2010). Beyond Rhodopsin: G Protein-Coupled Receptor Structure and Modeling Incorporating the β2-adrenergic and Adenosine A2A Crystal Structures. In: Bajorath, J. (eds) Chemoinformatics and Computational Chemical Biology. Methods in Molecular Biology, vol 672. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-60761-839-3_15

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  • DOI: https://doi.org/10.1007/978-1-60761-839-3_15

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-60761-838-6

  • Online ISBN: 978-1-60761-839-3

  • eBook Packages: Springer Protocols

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