4OL0

Crystal structure of transportin-SR2, a karyopherin involved in human disease, in complex with Ran

Summary for 4OL0

• Entry DOI: 10.2210/pdb4ol0/pdb
• Descriptor: GTP-binding nuclear protein Ran, Transportin-3, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: human karyopherins, active transport, nucleus, ran gtp-binding protein, protein transport
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P62826; Cytoplasm: Q9Y5L0
• Total number of polymer chains: 2
• Total formula weight: 129056.49

Authors

Tsirkone, V.G.,Strelkov, S.V. (deposition date: 2014-01-23, release date: 2014-04-09, Last modification date: 2024-02-28)

Primary citation

Tsirkone, V.G.,Beutels, K.G.,Demeulemeester, J.,Debyser, Z.,Christ, F.,Strelkov, S.V.
Structure of transportin SR2, a karyopherin involved in human disease, in complex with Ran.
Acta Crystallogr.,Sect.F, 70:723-729, 2014

PubMed 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.

PubMed: 24915079
DOI: 10.1107/S2053230X14009492

Experimental method

X-RAY DIFFRACTION (2.9 Å)