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Reference: Soniat M, et al. (2013) Crystal structure of human Karyopherin ?2 bound to the PY-NLS of Saccharomyces cerevisiae Nab2. J Struct Funct Genomics 14(2):31-5

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Abstract


Import-Karyopherin or Importin proteins bind nuclear localization signals (NLSs) to mediate the import of proteins into the cell nucleus. Karyopherin ?2 or Kap?2, also known as Transportin, is a member of this transporter family responsible for the import of numerous RNA binding proteins. Kap?2 recognizes a targeting signal termed the PY-NLS that lies within its cargos to target them through the nuclear pore complex. The recognition of PY-NLS by Kap?2 is conserved throughout eukaryotes. Kap104, the Kap?2 homolog in Saccharomyces cerevisiae, recognizes PY-NLSs in cargos Nab2, Hrp1, and Tfg2. We have determined the crystal structure of Kap?2 bound to the PY-NLS of the mRNA processing protein Nab2 at 3.05-? resolution. A seven-residue segment of the PY-NLS of Nab2 is observed to bind Kap?2 in an extended conformation and occupies the same PY-NLS binding site observed in other Kap?2?PY-NLS structures.

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Journal Article
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Soniat M, Sampathkumar P, Collett G, Gizzi AS, Banu RN, Bhosle RC, Chamala S, Chowdhury S, Fiser A, Glenn AS, ... Show all
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