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J Struct Funct Genomics. 2013 Jun;14(2):31-5. doi: 10.1007/s10969-013-9150-1. Epub 2013 Mar 28.

Crystal structure of human Karyopherin β2 bound to the PY-NLS of Saccharomyces cerevisiae Nab2.

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1
Department of Pharmacology, University of Texas Southwestern, Dallas, TX 75390, USA. michael.soniat@utsouthwestern.edu

Abstract

Import-Karyopherin or Importin proteins bind nuclear localization signals (NLSs) to mediate the import of proteins into the cell nucleus. Karyopherin β2 or Kapβ2, also known as Transportin, is a member of this transporter family responsible for the import of numerous RNA binding proteins. Kapβ2 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 Kapβ2 is conserved throughout eukaryotes. Kap104, the Kapβ2 homolog in Saccharomyces cerevisiae, recognizes PY-NLSs in cargos Nab2, Hrp1, and Tfg2. We have determined the crystal structure of Kapβ2 bound to the PY-NLS of the mRNA processing protein Nab2 at 3.05-Å resolution. A seven-residue segment of the PY-NLS of Nab2 is observed to bind Kapβ2 in an extended conformation and occupies the same PY-NLS binding site observed in other Kapβ2·PY-NLS structures.

PMID:
23535894
PMCID:
PMC3681870
DOI:
10.1007/s10969-013-9150-1
[Indexed for MEDLINE]
Free PMC Article
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