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• W2068722080 endingPage "638" @default.
• W2068722080 startingPage "628" @default.
• W2068722080 abstract "Conformational thermostabilisation of G-protein-coupled receptors is a successful strategy for their structure determination. The thermostable mutants tolerate short-chain detergents, such as octylglucoside and nonylglucoside, which are ideal for crystallography, and in addition, the receptors are preferentially in a single conformational state. The first thermostabilised receptor to have its structure determined was the β1-adrenoceptor mutant β1AR-m23 bound to the antagonist cyanopindolol, and recently, additional structures have been determined with agonist bound. Here, we describe further stabilisation of β1AR-m23 by the addition of three thermostabilising mutations (I129V, D322K, and Y343L) to make a mutant receptor that is 31 °C more thermostable than the wild-type receptor in dodecylmaltoside and is 13 °C more thermostable than β1AR-m23 in nonylglucoside. Although a number of thermostabilisation methods were tried, including rational design of disulfide bonds and engineered zinc bridges, the two most successful strategies to improve the thermostability of β1AR-m23 were an engineered salt bridge and leucine scanning mutagenesis. The three additional thermostabilising mutations did not significantly affect the pharmacological properties of β1AR-m23, but the new mutant receptor was significantly more stable in short-chain detergents such as heptylthioglucoside and denaturing detergents such as SDS." @default.
• W2068722080 created "2016-06-24" @default.
• W2068722080 creator A5039874120 @default.
• W2068722080 creator A5089964906 @default.
• W2068722080 date "2011-10-01" @default.
• W2068722080 modified "2023-09-23" @default.
• W2068722080 title "Engineering an Ultra-Thermostable β1-Adrenoceptor" @default.
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• W2068722080 doi "https://doi.org/10.1016/j.jmb.2011.08.057" @default.
• W2068722080 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3819908" @default.
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• W2068722080 hasPublicationYear "2011" @default.
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