Crystal structure of human Karyopherin beta 2 bound to the PY-NLS of Saccharomyces cerevisiae Nab2

Import-Karyopherin or Importin proteins bind nuclear localization signals (NLSs) to mediate the import of proteins into the cell nucleus. Karyopherin beta 2 or Kap beta 2, also known as Transportin, is a member of this transporter family responsible for the import of numerous RNA binding proteins. K...

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Published in:Journal of structural and functional genomics 2013-06, Vol.14 (2), p.31-35
Main Authors: Soniat, Michael, Sampathkumar, Parthasarathy, Collett, Garen, Gizzi, Anthony S, Banu, Radhika N, Bhosle, Rahul C, Chamala, Swetha, Chowdhury, Sukanya, Fiser, Andras, Glenn, Alan S, Hammonds, James, Hillerich, Brandan, Khafizov, Kamil, Love, James D, Matikainen, Bridget, Seidel, Ronald D, Toro, Rafael, Rajesh Kumar, P, Bonanno, Jeffery B, Chook, Yuh Min, Almo, Steven C
Format: Article
Language:English
Subjects:
Saccharomyces cerevisiae
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Summary:Import-Karyopherin or Importin proteins bind nuclear localization signals (NLSs) to mediate the import of proteins into the cell nucleus. Karyopherin beta 2 or Kap beta 2, also known as Transportin, is a member of this transporter family responsible for the import of numerous RNA binding proteins. Kap beta 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 beta 2 is conserved throughout eukaryotes. Kap104, the Kap beta 2 homolog in Saccharomyces cerevisiae, recognizes PY-NLSs in cargos Nab2, Hrp1, and Tfg2. We have determined the crystal structure of Kap beta 2 bound to the PY-NLS of the mRNA processing protein Nab2 at 3.05-Aa resolution. A seven-residue segment of the PY-NLS of Nab2 is observed to bind Kap beta 2 in an extended conformation and occupies the same PY-NLS binding site observed in other Kap beta 2.PY-NLS structures.
ISSN:1345-711X
1570-0267
DOI:10.1007/s10969-013-9150-1