GPCR Engineering Yields High-Resolution Structural Insights into β2-Adrenergic Receptor Function

@article{Rosenbaum2007GPCREY,
  title={GPCR Engineering Yields High-Resolution Structural Insights into $\beta$2-Adrenergic Receptor Function},
  author={Daniel M. Rosenbaum and Vadim Cherezov and Michael A. Hanson and S{\o}ren G. F. Rasmussen and Foon Sun Thian and Tong Sun Kobilka and Hee-Jung Choi and Xiao Jie Yao and William I. Weis and Raymond C. Stevens and Brian K. Kobilka},
  journal={Science},
  year={2007},
  volume={318},
  pages={1266 - 1273}
}
The β2-adrenergic receptor (β2AR) is a well-studied prototype for heterotrimeric guanine nucleotide–binding protein (G protein)–coupled receptors (GPCRs) that respond to diffusible hormones and neurotransmitters. To overcome the structural flexibility of the β2AR and to facilitate its crystallization, we engineered a β2AR fusion protein in which T4 lysozyme (T4L) replaces most of the third intracellular loop of the GPCR (“β2AR-T4L”) and showed that this protein retains near-native pharmacologic… Expand
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The Dynamic Process of β2-Adrenergic Receptor Activation
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High-Resolution Crystal Structure of an Engineered Human β2-Adrenergic G Protein–Coupled Receptor
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Although the location of carazolol in the β2-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 rhodopin as a template model for this large receptor family. Expand
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