title: Crystal structure of human Karyopherin β2 bound to the PY-NLS of Saccharomyces cerevisiae Nab2.
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.
authors.affiliation: Department of Pharmacology, University of Texas Southwestern, Dallas, TX 75390, USA. michael.soniat@utsouthwestern.edu
authors.forename: Michael
authors.initials: M
authors.lastname: Soniat
authors.forename: Parthasarathy
authors.initials: P
authors.lastname: Sampathkumar
authors.forename: Garen
authors.initials: G
authors.lastname: Collett
authors.forename: Anthony S
authors.initials: AS
authors.lastname: Gizzi
authors.forename: Radhika N
authors.initials: RN
authors.lastname: Banu
authors.forename: Rahul C
authors.initials: RC
authors.lastname: Bhosle
authors.forename: Swetha
authors.initials: S
authors.lastname: Chamala
authors.forename: Sukanya
authors.initials: S
authors.lastname: Chowdhury
authors.forename: Andras
authors.initials: A
authors.lastname: Fiser
authors.forename: Alan S
authors.initials: AS
authors.lastname: Glenn
authors.forename: James
authors.initials: J
authors.lastname: Hammonds
authors.forename: Brandan
authors.initials: B
authors.lastname: Hillerich
authors.forename: Kamil
authors.initials: K
authors.lastname: Khafizov
authors.forename: James D
authors.initials: JD
authors.lastname: Love
authors.forename: Bridget
authors.initials: B
authors.lastname: Matikainen
authors.forename: Ronald D
authors.initials: RD
authors.lastname: Seidel
authors.forename: Rafael
authors.initials: R
authors.lastname: Toro
authors.forename: P
authors.initials: P
authors.lastname: Rajesh Kumar
authors.forename: Jeffery B
authors.initials: JB
authors.lastname: Bonanno
authors.forename: Yuh Min
authors.initials: YM
authors.lastname: Chook
authors.forename: Steven C
authors.initials: SC
authors.lastname: Almo
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002467:Cell Nucleus / Q000378:metabolism; D018360:Crystallography, X-Ray; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D019913:Nuclear Localization Signals / Q000737:chemistry* / Q000378:metabolism; D029543:Nucleocytoplasmic Transport Proteins / Q000737:chemistry* / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism; D028961:beta Karyopherins / Q000737:chemistry* / Q000378:metabolism
chemical_list: C080773:NAB2 protein, S cerevisiae; D019913:Nuclear Localization Signals; D029543:Nucleocytoplasmic Transport Proteins; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D029701:Saccharomyces cerevisiae Proteins; C108121:TNPO1 protein, human; D028961:beta Karyopherins
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