Literature DB >> 10367892

Structural view of the Ran-Importin beta interaction at 2.3 A resolution.

I R Vetter1, A Arndt, U Kutay, D Görlich, A Wittinghofer.   

Abstract

Transport receptors of the Importin beta family shuttle between the nucleus and cytoplasm and mediate transport of macromolecules through nuclear pore complexes. They interact specifically with the GTP-binding protein Ran, which in turn regulates their interaction with cargo. Here, we report the three-dimensional structure of a complex between Ran bound to the nonhydrolyzable GTP analog GppNHp and a 462-residue fragment from Importin beta. The structure of Importin beta shows 10 tandem repeats resembling HEAT and Armadillo motifs. They form an irregular crescent, the concave site of which forms the interface with Ran-triphosphate. The importin-binding site of Ran does not overlap with that of the Ran-binding domain of RanBP2.

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Year:  1999        PMID: 10367892     DOI: 10.1016/s0092-8674(00)80774-6

Source DB:  PubMed          Journal:  Cell        ISSN: 0092-8674            Impact factor:   41.582


  96 in total

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Journal:  Protein Sci       Date:  2004-03       Impact factor: 6.725

5.  The Noc proteins involved in ribosome synthesis and export contain divergent HEAT repeats.

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Journal:  RNA       Date:  2004-03       Impact factor: 4.942

6.  Direct discrimination between models of protein activation by single-molecule force measurements.

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7.  Weak conservation of structural features in the interfaces of homologous transient protein-protein complexes.

Authors:  Govindarajan Sudha; Prashant Singh; Lakshmipuram S Swapna; Narayanaswamy Srinivasan
Journal:  Protein Sci       Date:  2015-09-08       Impact factor: 6.725

8.  Sumoylation of the GTPase Ran by the RanBP2 SUMO E3 Ligase Complex.

Authors:  Volkan Sakin; Sebastian M Richter; He-Hsuan Hsiao; Henning Urlaub; Frauke Melchior
Journal:  J Biol Chem       Date:  2015-08-06       Impact factor: 5.157

9.  Modeling Huntington's disease in cells, flies, and mice.

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10.  Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex.

Authors:  Shuya Fukai; Hugo T Matern; Junutula R Jagath; Richard H Scheller; Axel T Brunger
Journal:  EMBO J       Date:  2003-07-01       Impact factor: 11.598

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