1o6p
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1o6p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o6p, resolution 2.8Å" /> '''IMPORTIN BETA BOUND ...)
Next diff →
Revision as of 16:23, 12 November 2007
|
IMPORTIN BETA BOUND TO A GLFG NUCLEOPORIN PEPTIDE
Overview
The interaction between nuclear pore proteins (nucleoporins) and transport, factors is crucial for the translocation of macromolecules through nuclear, pores. Many nucleoporins contain FG sequence repeats, and previous studies, have demonstrated interactions between repeats containing FxFG or GLFG, cores and transport factors. The crystal structure of residues 1-442 of, importin-beta bound to a GLFG peptide indicates that this repeat core, binds to the same primary site as FxFG cores. Importin-beta-I178D shows, reduced binding to both FxFG and GLFG repeats, consistent with both, binding to an overlapping site in the hydrophobic groove between the, A-helices of HEAT repeats 5 and 6. Moreover, FxFG repeats can displace, importin-beta or its S. cerevisiae homologue, Kap95, bound to GLFG, repeats. Addition of soluble GLFG repeats decreases the rate of nuclear, protein import in digitonin-permeabilized HeLa cells, indicating that this, interaction has a role in the translocation of carrier-cargo complexes, through nuclear pores. The binding of GLFG and FxFG repeats to overlapping, sites on importin-beta indicates that functional differences between, different repeats probably arise from differences in their spatial, organization.
About this Structure
1O6P is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta., Bayliss R, Littlewood T, Strawn LA, Wente SR, Stewart M, J Biol Chem. 2002 Dec 27;277(52):50597-606. Epub 2002 Oct 7. PMID:12372823
Page seeded by OCA on Mon Nov 12 18:30:11 2007
