Kawato Tatsuya, Mizohata Eiichi, Shimizu Yohei, Meshizuka Tomohiro, Yamamoto Tomohiro, Takasu Noriaki, Matsuoka Masahiro, Matsumura Hiroyoshi, Kodama Tatsuhiko, Kanai Motomu, Doi Hirofumi, Inoue Tsuyoshi, Sugiyama Akira
a Division of Applied Chemistry, Graduate School of Engineering , Osaka University , Suita , Japan.
Biosci Biotechnol Biochem. 2015;79(4):640-2. doi: 10.1080/09168451.2014.991692. Epub 2015 Jan 3.
The streptavidin/biotin interaction has been widely used as a useful tool in research fields. For application to a pre-targeting system, we previously developed a streptavidin mutant that binds to an iminobiotin analog while abolishing affinity for natural biocytin. Here, we design a bivalent iminobiotin analog that shows 1000-fold higher affinity than before, and determine its crystal structure complexed with the mutant protein.
链霉亲和素/生物素相互作用已在研究领域中被广泛用作一种有用的工具。为了应用于预靶向系统，我们之前开发了一种链霉亲和素突变体，它能与亚氨基生物素类似物结合，同时消除对天然生物胞素的亲和力。在此，我们设计了一种二价亚氨基生物素类似物，其亲和力比之前高出1000倍，并确定了它与突变蛋白复合的晶体结构。
