Tsirkone Vicky G, Beutels Katrien G, Demeulemeester Jonas, Debyser Zeger, Christ Frauke, Strelkov Sergei V
Laboratory for Biocrystallography, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven, Herestraat 49 bus 822, 3000 Leuven, Belgium.
Laboratory of Molecular Virology and Gene Therapy, Department of Pharmaceutical and Pharmacological Sciences, KU Leuven, Herestraat 49 bus 822, 3000 Leuven, Belgium.
Acta Crystallogr F Struct Biol Commun. 2014 Jun;70(Pt 6):723-9. doi: 10.1107/S2053230X14009492. Epub 2014 May 24.
Transportin SR2 (TRN-SR2) is a β-type karyopherin responsible for the nuclear import of specific cargoes, including serine/arginine-rich splicing factors. The protein has been implicated in a variety of human diseases, including HIV infection, primary biliary cirrhosis and limb-girdle muscular dystrophy 1F. Towards understanding its molecular mechanism, a 2.9 Å resolution crystal structure of human TRN-SR2 complexed with the small GTPase Ran has been determined. TRN-SR2 is composed of 20 α-helical HEAT repeats forming a solenoid-like fold. The first nine repeats form a `cradle' for the binding of RanGTP, revealing similarities but also differences with respect to the related importin 13 complex.
转运蛋白SR2(TRN-SR2)是一种β型核转运蛋白,负责特定货物的核输入,包括富含丝氨酸/精氨酸的剪接因子。该蛋白与多种人类疾病有关,包括HIV感染、原发性胆汁性肝硬化和1F型肢带型肌营养不良症。为了了解其分子机制,已确定了与小GTP酶Ran复合的人TRN-SR2的2.9Å分辨率晶体结构。TRN-SR2由20个α螺旋HEAT重复序列组成,形成类似螺线管的折叠结构。前九个重复序列形成一个用于结合RanGTP的“摇篮”,揭示了与相关输入蛋白13复合物的相似性和差异。