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Structure of transportin SR2, a karyopherin involved in human disease, in complex with Ran.


ABSTRACT: Transportin SR2 (TRN-SR2) is a ?-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 ?-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.

SUBMITTER: Tsirkone VG 

PROVIDER: S-EPMC4051523 | biostudies-literature | 2014 Jun

REPOSITORIES: biostudies-literature

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Structure of transportin SR2, a karyopherin involved in human disease, in complex with Ran.

Tsirkone Vicky G VG   Beutels Katrien G KG   Demeulemeester Jonas J   Debyser Zeger Z   Christ Frauke F   Strelkov Sergei V SV  

Acta crystallographica. Section F, Structural biology communications 20140524 Pt 6


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-helic  ...[more]

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