4JLQ

Crystal structure of human Karyopherin-beta2 bound to the PY-NLS of Saccharomyces cerevisiae NAB2

Replaces:  4H1K

Summary for 4JLQ

• Entry DOI: 10.2210/pdb4jlq/pdb
• Descriptor: Transportin-1, Nuclear polyadenylated RNA-binding protein NAB2 (2 entities in total)
• Functional Keywords: heat repeats, karyopherin, nuclear import, proteintransport, importin, transportin, transport protein, nls, nab2, structural genomics, nucleocytoplasmic transport: a target for cellular control (npcxstals), new york structural genomics research consortium (nysgrc), psi-biology, npcxstals
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q92973; Nucleus: P32505
• Total number of polymer chains: 2
• Total formula weight: 100790.23

Authors

Sampathkumar, P.,Gizzi, A.,Rout, M.P.,Chook, Y.M.,Almo, S.C.,New York Structural Genomics Research Consortium (NYSGRC),Nucleocytoplasmic Transport: a Target for Cellular Control (NPCXstals) (deposition date: 2013-03-12, release date: 2013-04-03, Last modification date: 2023-09-20)

Primary citation

Soniat, M.,Sampathkumar, P.,Collett, G.,Gizzi, A.S.,Banu, R.N.,Bhosle, R.C.,Chamala, S.,Chowdhury, S.,Fiser, A.,Glenn, A.S.,Hammonds, J.,Hillerich, B.,Khafizov, K.,Love, J.D.,Matikainen, B.,Seidel, R.D.,Toro, R.,Rajesh Kumar, P.,Bonanno, J.B.,Chook, Y.M.,Almo, S.C.
Crystal structure of human Karyopherin beta 2 bound to the PY-NLS of Saccharomyces cerevisiae Nab2.
J.Struct.Funct.Genom., 14:31-35, 2013

PubMed 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.

PubMed: 23535894
DOI: 10.1007/s10969-013-9150-1

Experimental method

X-RAY DIFFRACTION (3.05 Å)