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Crystal structure of mammalian casein kinase I exhibits basis for phosphate recognition by a protein kinase family.

机译:哺乳动物酪蛋白激酶I的晶体结构显示了蛋白激酶家族识别磷酸盐的基础。

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摘要

Casein kinase I (CKI) enzymes phosphorylate multiple proteins with diverse functions in eukaryotic organisms and may play an important regulatory role in a variety of biological processes. These protein kinases utilize ATP in a reaction forming a phosphate mono-ester that typically can be hydrolyzed by a protein phosphatase. Common features of certain substrates show that CKI activity has an unusual specificity for proteins that are already phosphorylated on an amino acid N-terminal to the site phosphorylated by CKI. Recently, cDNAs encoding several CKI enzymes have been cloned. Sequence analysis reveals that these enzymes constitute a unique family of protein kinases. While their catalytic domains have many similarities, regions outside of this domain vary in length and sequence.;To understand the molecular basis for protein phosphorylation by CKI enzymes, experiments were designed to study the three-dimensional structure of a recombinant mammalian isoform of CKI expressed in Escherichia coli. Crystals of a truncation mutant of CKI
机译:酪蛋白激酶I(CKI)酶使真核生物中具有多种功能的多种蛋白质磷酸化,并可能在多种生物学过程中发挥重要的调节作用。这些蛋白激酶在形成磷酸单酯的反应中利用ATP,该磷酸单酯通常可以被蛋白磷酸酶水解。某些底物的共同特征表明,CKI活性对已经在CKI磷酸化位点的N端氨基酸上磷酸化的蛋白质具有异常的特异性。最近,已经克隆了编码几种CKI酶的cDNA。序列分析表明,这些酶构成了独特的蛋白激酶家族。尽管它们的催化结构域具有许多相似性,但该结构域之外的区域的长度和序列却有所不同。为了了解CKI酶使蛋白质磷酸化的分子基础,设计了实验来研究表达的CKI重组哺乳动物同工型的三维结构在大肠杆菌中。 CKI截短突变体的晶体

著录项

  • 作者

    Longenecker, Kenton Lamar.;

  • 作者单位

    Indiana University.;

  • 授予单位 Indiana University.;
  • 学科 Chemistry Biochemistry.;Biophysics Medical.
  • 学位 Ph.D.
  • 年度 1997
  • 页码 160 p.
  • 总页数 160
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

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