1f59

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(New page: 200px<br /> <applet load="1f59" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f59, resolution 2.8&Aring;" /> '''IMPORTIN-BETA-FXFG N...)
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Revision as of 14:42, 12 November 2007

Image:1f59.gif

1f59, resolution 2.8Å

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IMPORTIN-BETA-FXFG NUCLEOPORIN COMPLEX

Overview

We describe the crystal structure of a complex between importin-beta, residues 1-442 (Ib442) and five FxFG nucleoporin repeats from Nsp1p., Nucleoporin FxFG cores bind on the convex face of Ib442 to a primary site, between the A helices of HEAT repeats 5 and 6, and to a secondary site, between HEAT repeats 6 and 7. Mutations at importin-beta Ile178 in the, primary FxFG binding site reduce both binding and nuclear protein import, providing direct evidence for the functional significance of the, importin-beta-FxFG interaction. The FxFG binding sites on importin-beta do, not overlap with the RanGTP binding site. Instead, RanGTP may release, importin-beta from FxFG nucleoporins by generating a conformational change, that alters the structure of the FxFG binding site.

About this Structure

1F59 is a Single protein structure of sequence from Homo sapiens and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking., Bayliss R, Littlewood T, Stewart M, Cell. 2000 Jul 7;102(1):99-108. PMID:10929717

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