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Crystal structure of transportin-SR2, a karyopherin involved in human disease, in complex with RanCrystal structure of transportin-SR2, a karyopherin involved in human disease, in complex with Ran
Structural highlights
FunctionRAN_HUMAN GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2.[1] [2] [3] [4] Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.[5] [6] [7] [8] Publication Abstract from PubMedTransportin SR2 (TRN-SR2) is a beta-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 A resolution crystal structure of human TRN-SR2 complexed with the small GTPase Ran has been determined. TRN-SR2 is composed of 20 alpha-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. Structure of transportin SR2, a karyopherin involved in human disease, in complex with Ran.,Tsirkone VG, Beutels KG, Demeulemeester J, Debyser Z, Christ F, Strelkov SV Acta Crystallogr F Struct Biol Commun. 2014 Jun;70(Pt 6):723-9. doi:, 10.1107/S2053230X14009492. Epub 2014 May 24. PMID:24915079[9] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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