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Crystal structure of the WD40 domain of human PRPF19.
Zhang, Yuzhe; Li, Yue; Liang, Xiao; Zhu, Zhongliang; Sun, Hongbin; He, Hao; Min, Jinrong; Liao, Shanhui; Liu, Yanli.
Afiliação
  • Zhang Y; Hubei Key Laboratory of Genetic Regulation and Integrative Biology, School of Life Sciences, Central China Normal University, Wuhan 430079, PR China; Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7, Canada; Yunnan Provincial Key Laboratory of Entomological Biopharmace
  • Li Y; School of Life Sciences, University of Science and Technology of China, Hefei 230027, PR China.
  • Liang X; Hubei Key Laboratory of Genetic Regulation and Integrative Biology, School of Life Sciences, Central China Normal University, Wuhan 430079, PR China.
  • Zhu Z; School of Life Sciences, University of Science and Technology of China, Hefei 230027, PR China.
  • Sun H; High Magnetic Field Laboratory, Hefei Institutes of Physical Science, Academy of Sciences of China, Hefei 230031, PR China.
  • He H; Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
  • Min J; Hubei Key Laboratory of Genetic Regulation and Integrative Biology, School of Life Sciences, Central China Normal University, Wuhan 430079, PR China; Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
  • Liao S; School of Life Sciences, University of Science and Technology of China, Hefei 230027, PR China. Electronic address: ajsod@mail.ustc.edu.cn.
  • Liu Y; Hubei Key Laboratory of Genetic Regulation and Integrative Biology, School of Life Sciences, Central China Normal University, Wuhan 430079, PR China; Structural Genomics Consortium, University of Toronto, Toronto, Ontario M5G 1L7, Canada. Electronic address: yanliliu@mail.ccnu.edu.cn.
Biochem Biophys Res Commun ; 493(3): 1250-1253, 2017 11 25.
Article em En | MEDLINE | ID: mdl-28962858
ABSTRACT
Human Pre-mRNA Processing factor 19 (hPRPF19) is an important component in human spliceosome machinery. hPRPF19 contains a WD40 repeats domain at its C-terminus, which is also conserved in yeast. Here we determined the crystal structure of the C-terminal WD40 repeat domain of hPRPF19 by X-ray crystallography. Our structural analysis revealed some significantly different structure features between the human and yeast Prp19 WD40 repeat domain. However, there are also conserved clusters of residues at the bottom surface of the fourth and the fifth WD40 repeats, which provides the important implication for the conserved Prp19 proteins in both human and yeast.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas Nucleares / Enzimas Reparadoras do DNA / Fatores de Processamento de RNA Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas Nucleares / Enzimas Reparadoras do DNA / Fatores de Processamento de RNA Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Ano de publicação: 2017 Tipo de documento: Article