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Structure-based design of a pathway-specific nuclear import inhibitor.

ABSTRACT: Kapbeta2 (also called transportin) recognizes PY nuclear localization signal (NLS), a new class of NLS with a R/H/Kx((2-5))PY motif. Here we show that Kapbeta2 complexes containing hydrophobic and basic PY-NLSs, as classified by the composition of an additional N-terminal motif, converge in structure only at consensus motifs, which explains ligand diversity. On the basis of these data and complementary biochemical analyses, we designed a Kapbeta2-specific nuclear import inhibitor, M9M.

SUBMITTER: Cansizoglu AE

PROVIDER: S-EPMC3437620 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature

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Structure-based design of a pathway-specific nuclear import inhibitor.

Cansizoglu Ahmet E AE Lee Brittany J BJ Zhang Zi Chao ZC Fontoura Beatriz M A BM Chook Yuh Min YM

Nature structural & molecular biology 20070415 5

Kapbeta2 (also called transportin) recognizes PY nuclear localization signal (NLS), a new class of NLS with a R/H/Kx((2-5))PY motif. Here we show that Kapbeta2 complexes containing hydrophobic and basic PY-NLSs, as classified by the composition of an additional N-terminal motif, converge in structure only at consensus motifs, which explains ligand diversity. On the basis of these data and complementary biochemical analyses, we designed a Kapbeta2-specific nuclear import inhibitor, M9M. ...[more]

PMID: 17435768

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