N-Terminal T4 Lysozyme Fusion Facilitates Crystallization of a G Protein Coupled Receptor |
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| Authors: | Yaozhong Zou William I. Weis Brian K. Kobilka |
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| Affiliation: | 1. Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California, United States of America.; 2. Department of Structural Biology, Stanford University School of Medicine, Stanford, California, United States of America.; Medical School of Hannover, United States of America, |
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| Abstract: | A highly crystallizable T4 lysozyme (T4L) was fused to the N-terminus of the β2 adrenergic receptor (β2AR), a G-protein coupled receptor (GPCR) for catecholamines. We demonstrate that the N-terminal fused T4L is sufficiently rigid relative to the receptor to facilitate crystallogenesis without thermostabilizing mutations or the use of a stabilizing antibody, G protein, or protein fused to the 3rd intracellular loop. This approach adds to the protein engineering strategies that enable crystallographic studies of GPCRs alone or in complex with a signaling partner. |
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