Michael Soniat, Parthasarathy Sampathkumar, Garen Collett, Anthony S Gizzi, Radhika N Banu, Rahul C Bhosle, Swetha Chamala, Sukanya Chowdhury, Andras Fiser, Alan S Glenn, James Hammonds, Brandan Hillerich, Kamil Khafizov, James D Love, Bridget Matikainen, Ronald D Seidel, Rafael Toro, P Rajesh Kumar, Jeffery B Bonanno, Yuh Min Chook, Steven C Almo
{"title":"人核粘蛋白β2与酿酒酵母Nab2蛋白PY-NLS结合的晶体结构。","authors":"Michael Soniat, Parthasarathy Sampathkumar, Garen Collett, Anthony S Gizzi, Radhika N Banu, Rahul C Bhosle, Swetha Chamala, Sukanya Chowdhury, Andras Fiser, Alan S Glenn, James Hammonds, Brandan Hillerich, Kamil Khafizov, James D Love, Bridget Matikainen, Ronald D Seidel, Rafael Toro, P Rajesh Kumar, Jeffery B Bonanno, Yuh Min Chook, Steven C Almo","doi":"10.1007/s10969-013-9150-1","DOIUrl":null,"url":null,"abstract":"<p><p>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.</p>","PeriodicalId":73957,"journal":{"name":"Journal of structural and functional genomics","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2013-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/s10969-013-9150-1","citationCount":"23","resultStr":"{\"title\":\"Crystal structure of human Karyopherin β2 bound to the PY-NLS of Saccharomyces cerevisiae Nab2.\",\"authors\":\"Michael Soniat, Parthasarathy Sampathkumar, Garen Collett, Anthony S Gizzi, Radhika N Banu, Rahul C Bhosle, Swetha Chamala, Sukanya Chowdhury, Andras Fiser, Alan S Glenn, James Hammonds, Brandan Hillerich, Kamil Khafizov, James D Love, Bridget Matikainen, Ronald D Seidel, Rafael Toro, P Rajesh Kumar, Jeffery B Bonanno, Yuh Min Chook, Steven C Almo\",\"doi\":\"10.1007/s10969-013-9150-1\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>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.</p>\",\"PeriodicalId\":73957,\"journal\":{\"name\":\"Journal of structural and functional genomics\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2013-06-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1007/s10969-013-9150-1\",\"citationCount\":\"23\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of structural and functional genomics\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1007/s10969-013-9150-1\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2013/3/28 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of structural and functional genomics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/s10969-013-9150-1","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2013/3/28 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}
Crystal structure of human Karyopherin β2 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 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.
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