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

Acta Crystallogr F Struct Biol Commun. 2014 Jun;70(Pt 6):723-9. doi: 10.1107/S2053230X14009492. Epub 2014 May 24.

Abstract

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.

Keywords: molecular mechanism; nuclear import; transportin SR2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Humans
  • Molecular Sequence Data
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • beta Karyopherins / chemistry*
  • ran GTP-Binding Protein / chemistry*

Substances

  • RAN protein, human
  • beta Karyopherins
  • transportin SR2
  • ran GTP-Binding Protein

Associated data

  • PDB/4O10