• Search Research Projects
  • Search Researchers
  • How to Use
  1. Back to previous page

Structural analysis of sulfotransferase

Research Project

Project/Area Number 16K07273
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeMulti-year Fund
Section一般
Research Field Structural biochemistry
Research InstitutionKyushu University

Principal Investigator

Yoshimitsu Kakuta  九州大学, 農学研究院, 教授 (00314360)

Project Period (FY) 2016-04-01 – 2019-03-31
Project Status Completed (Fiscal Year 2019)
Budget Amount *help
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2018: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2017: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2016: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Keywords硫酸転移酵素 / 結晶構造解析 / タンパク質チロシン硫酸化 / 蛋白質 / 酵素反応 / 構造解析
Outline of Final Research Achievements

To clarify the detailed molecular mechanism of sulfation of a tyrosine residue, which is one of the post-translational modifications of proteins, the three-dimensional structure analysis of tyrosylprotein sulfotransferase (TPST) was done.
We have determined crystal structure of human tyrosyltransfease-1 using X-ray crystalography. This provided a lot of information on the molecular mechanism of the substrate recognition function of TPST.

Academic Significance and Societal Importance of the Research Achievements

ヒト硫酸転移酵素の立体構造情報を得たことにより、主要なタンパク質の翻訳後修飾の一つであるチロシン残基の硫酸化の詳細な分子メカニズムを明らかにすることができた。多くのタンパク質はチロシン残基が硫酸化することにより、その生理活性が変化する。今回の情報から、この反応を人工的に制御できる可能性が高まったことから、今後の多くの展開が期待できる。

Report

(2 results)
  • 2019 Final Research Report ( PDF )
  • 2016 Research-status Report
  • Research Products

    (1 results)

All 2016

All Presentation (1 results)

  • [Presentation] 翻訳後修飾を行うヒトタンパク質チロシン硫酸転移酵素の結晶構造解析2016

    • Author(s)
      角田佳充
    • Organizer
      日本蛋白質科学会年会
    • Place of Presentation
      福岡国際会議場
    • Related Report
      2016 Research-status Report

URL: 

Published: 2016-04-21   Modified: 2025-01-30  

Information User Guide FAQ News Terms of Use Attribution of KAKENHI

Powered by NII kakenhi