1un0
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CRYSTAL STRUCTURE OF YEAST KARYOPHERIN (IMPORTIN) ALPHA IN COMPLEX WITH A NUP2P N-TERMINAL FRAGMENT
OverviewOverview
The yeast nucleoporin Nup2p is associated primarily with the nuclear, basket of nuclear pore complexes and is required for efficient, importin-alpha:beta-mediated nuclear protein import as well as efficient, nuclear export of Kap60p/importin-alpha. Residues 1-51 of Nup2p bind, tightly to Kap60p and are required for Nup2p function in vivo. We have, determined the 2.6 A resolution crystal structure of a complex between, this region of Nup2p and the armadillo repeat domain of Kap60p. Nup2p, binds along the inner concave groove of Kap60p, but its interaction, interface is different from that employed for nuclear localization signal, (NLS) recognition although there is some overlap between them. Nup2p binds, Kap60p more strongly than NLSs and accelerates release of NLSs from, Kap60p. Nup2p itself is released from Kap60p by Cse1p:RanGTP only in the, presence of the importin-beta binding (IBB) domain of Kap60p. These data, indicate that Nup2p increases the overall rate of nuclear trafficking by, coordinating nuclear import termination and importin recycling as a, concerted process.
About this StructureAbout this Structure
1UN0 is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import., Matsuura Y, Lange A, Harreman MT, Corbett AH, Stewart M, EMBO J. 2003 Oct 15;22(20):5358-69. PMID:14532109
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