一种作为亲和捕获试剂设计的重复蛋白。
A designed repeat protein as an affinity capture reagent.
作者信息
Speltz Elizabeth B, Brown Rebecca S H, Hajare Holly S, Schlieker Christian, Regan Lynne
机构信息
Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06511, U.S.A.
Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06511, U.S.A. Integrated Graduate Program in Physical and Engineering Biology, Yale University, 266 Whitney Avenue, New Haven, CT 06511, U.S.A. Department of Chemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06511, U.S.A.
出版信息
Biochem Soc Trans. 2015 Oct;43(5):874-80. doi: 10.1042/BST20150091.
Repeat proteins are an attractive target for protein engineering and design. We have focused our attention on the design and engineering of one particular class: tetratricopeptide repeat (TPR) proteins. In previous work, we have shown that the structure and stability of TPR proteins can be manipulated in a rational fashion [Cortajarena (2011) Prot. Sci. 20: , 1042-1047; Main (2003) Structure 11: , 497-508]. Building on those studies, we have designed and characterized a number of different peptide-binding TPR modules and we have also assembled these modules into supramolecular arrays [Cortajarena (2009) ACS Chem. Biol. 5: , 545-552; Cortajarena (2008) ACS Chem. Biol. 3: , 161-166; Jackrel (2009) Prot. Sci. 18: , 762-774; Kajander (2007) Acta Crystallogr. D Biol. Crystallogr. 63: , 800-811]. Here we focus on the development of one such TPR-peptide interaction for a practical application, affinity purification. We illustrate the general utility of our designed protein interaction. Furthermore, this example highlights how basic research on protein-peptide interactions can lead to the development of novel reagents with important practical applications.
重复蛋白是蛋白质工程和设计的一个有吸引力的目标。我们将注意力集中在一类特定蛋白的设计和工程上：四肽重复序列（TPR）蛋白。在之前的工作中，我们已经表明TPR蛋白的结构和稳定性可以通过合理的方式进行调控[Cortajarena（2011年）《蛋白质科学》20：，1042 - 1047；Main（2003年）《结构》11：，497 - 508]。基于这些研究，我们设计并表征了许多不同的肽结合TPR模块，并且我们还将这些模块组装成了超分子阵列[Cortajarena（2009年）《美国化学会化学生物学》5：，545 - 552；Cortajarena（2008年）《美国化学会化学生物学》3：，161 - 166；Jackrel（2009年）《蛋白质科学》18：，762 - 774；Kajander（2007年）《晶体学报D辑：生物晶体学》63：，800 - 811]。在这里，我们专注于开发一种这样的TPR - 肽相互作用以用于实际应用，即亲和纯化。我们阐述了我们设计的蛋白质相互作用的一般实用性。此外，这个例子突出了关于蛋白质 - 肽相互作用的基础研究如何能够导致具有重要实际应用的新型试剂的开发。
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