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Relation between the structure and function of proteins studied by the changes of tyrosine and tryptophan residues.

Research Project

Project/Area Number 14570103
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field General medical chemistry
Research InstitutionHosei University (2004)
Kanazawa University (2002-2003)

Principal Investigator

NAGAI Masako  Hosei University, College of Technology, Visiting Professor, 工学部, 客員教授 (60019578)

Co-Investigator(Kenkyū-buntansha) SAKURAI Hiroshi  Kanazawa University, School of Medicine, Professor (2002-,2003), 医学部, 助教授 (00225848)
IMAI Kiyohiro  Hosei University, College of Technology, Professor (2004), 工学部, 教授 (50028528)
Project Period (FY) 2002 – 2004
Project Status Completed (Fiscal Year 2004)
Budget Amount *help
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 2004: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 2003: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 2002: ¥1,700,000 (Direct Cost: ¥1,700,000)
Keywordshemoglobin / SH3 / near-UV CD / UV resonance Raman / mutants / tyrosine / tryptophan / quaternary structure transition / 高次構造変化 / 芳香族アミノ酸 / 酸素結合機能 / CD / 共鳴ラマン / HbM / アロステリックエフェクター / 蛋白質の機能 / 円二色性(CD) / PI3K / 異常血色素 / SrcSH3 domein / 共鳴ラマン分光 / 円二色性
Research Abstract

To get insight into how the quaternary structure changes correlate to their functions, we examined the near-UV CD and UV resonance Raman spectra of hemoglobin and the domein of Src-homology-3 protein with and without ligands. Using four newly synthesized mutant hemoglobins at α42Tyr,α140Tyr,β145Tyr, and/or β37Trp, it was clarified that the main contributors for a negative CD band, a T-sate marker band, are α140Tyr and β145Tyr, located at C-terminal positions. The T-structure specific UV resonance Raman bands of Tyr and Trp were characterized using a natural mutant Hb, Hb M Boston and a Ni-Fe Hybrid hemoglobin.
Src-homology-3(SH3) protein recognize a Pro rich peptides and communicate with the other proteins. We demonstrated that SH3 interacts to the ligand peptide via Tyr residue(s) using UV CD and UV resonance Raman spectoscopy. SH3 has six Tyr residues. Specific Tyr residue for the interaction with Pro-rich peptide was specified as 14Tyr using mutants synthesized in E.coli each Tyr replaced by Ala. Interestingly, Src-SH3 and PI3K-SH3 showed different shtructure changes with the interaction of ligand peptides reflecting the different protein recognition.

Report

(4 results)
  • 2004 Annual Research Report   Final Research Report Summary
  • 2003 Annual Research Report
  • 2002 Annual Research Report
  • Research Products

    (21 results)

All 2004 2003 2002 Other

All Journal Article (14 results) Publications (7 results)

  • [Journal Article] Changes of near-UV CD spectrum of human hemoglobin upon oxygen binding : A study of mutants at α42, α140, β145 Tyr or β37 Trp.2004

    • Author(s)
      Jin, Y., Sakurai, H., Nagai, Y., Nagai, M.
    • Journal Title

      Biopolymers 74

      Pages: 60-63

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Heme structures of five variants of Hemoglobin M probed by resonance Raman spectroscopy.2004

    • Author(s)
      Jin, Y., Nagai, M., Nagai, Y., Nagatomo, S., Kitagawa, T.
    • Journal Title

      Biochemistry 43

      Pages: 8517-8527

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Changes of near-UV CD spectrum of human hemoglobin upon oxygen binding : A study of mutants at α42,α140,β145 tyrosine or β37 tryptophan.2004

    • Author(s)
      Jin, Y., Sakurai, H., Nagai, Y., Nagai, M.
    • Journal Title

      Biopolymers 74

      Pages: 60-63

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Heme structures of five variants of hemoglobin M probed by resonance Raman spectroscopy.2004

    • Author(s)
      Jin, Y., Nagai, M., Nagai, Y., Nagatomo, S., Kitagawa, T.
    • Journal Title

      Biochemistry 43

      Pages: 8517-8527

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Changes of near-UV CD spectrum of human hemoglobin upon oxygen binding : A study of mutants at α42,α140,β145Tyr and β37 Trp..2004

    • Author(s)
      Jin, Y., Sakurai, H., Nagai, Y., Nagai, M.
    • Journal Title

      Biopolymers 74

      Pages: 60-63

    • Related Report
      2004 Annual Research Report
  • [Journal Article] Heme structure of five variants of Hb M probed by resonance Raman spectroscopy.2004

    • Author(s)
      Jin, Y., Nagai, M., Nagai, Y., Nagatomo, S., Kitagawa, T.
    • Journal Title

      Biochemistry 43(26)

      Pages: 8517-8527

    • Related Report
      2004 Annual Research Report
  • [Journal Article] Differential ligand recognition by the Src and PI3K Src homology 3 domeins : CD and UV resonance Raman studies.2003

    • Author(s)
      Okishio, N., Tanaka, T., Fukuda, R., Nagai, M.
    • Journal Title

      Biochemistry 42

      Pages: 208-216

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Different ligand recognition by the Src and PI3K Src homology 3 domeins : CD and UV resonance Raman studies2003

    • Author(s)
      Okishio, N., Tanaka, T., Fukuda, R., Nagai, M.
    • Journal Title

      Biochemistry 42

      Pages: 208-216

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Changes in the abnormal α-subunit upon CO-binding to the normal β-subunit of Hb M Boston : resonance Raman, EPR and CD study.2002

    • Author(s)
      Nagatomo, S., Jin, Y., Nagai, M., Hori, H., Kitagawa, T.
    • Journal Title

      Biophysical Chemistry 98

      Pages: 217-232

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Differences in changes of the α1-β2 subunit contacts between ligand binding to the α and β subunits of Hb A : UV resonance Raman analysis using Ni-Fe hybrid hemoglobin.2002

    • Author(s)
      Nagatomo, S., Nagai, M., Shibayama, N., Kitagawa, T.
    • Journal Title

      Biochemistry 41

      Pages: 10010-10020

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Changes in the abnormal α-subunit upon CO-binding to the normal β-subunit of Hb M Boston : resonance Raman, EPR, and CD study.2002

    • Author(s)
      Nagatomo, S., Jin, Y., Nagai, M., Hori, H., Kitagawa, T.
    • Journal Title

      Biophysical Chemistry 98

      Pages: 217-232

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Differences in changes of the α1β2 subunit contacts between ligand binding to the α and β subunits of Hb A. UV resonance Raman analysis using Ni-Fe hybrid hemoglobin2002

    • Author(s)
      Nagatomo, S., Nagai, M., Shibayama, N., Kitagawa, T.
    • Journal Title

      Biochemistry 41

      Pages: 10010-10020

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Quaternary structures of intermediately liganded human hemoglobin A and influences from strong allosteric effectors ; resonance Raman investigation.

    • Author(s)
      Nagatomo, S., Nagai, M., Mizutani, Y., Yonetani, T., Kitagawa, T.
    • Journal Title

      (投稿中)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Journal Article] Quaternary structures of intermediately liganded human hemoglobin A and influences from strong allosteric effectors ; resonance Raman investigation.

    • Author(s)
      Nagatomo, S., Nagai, M., Mizutani, Y., Yonetani, T., Kttagawa, T.
    • Journal Title

      (Submitted)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      2004 Final Research Report Summary
  • [Publications] Jin, Y., Sakurai, H., Nagai, Y., Nagai, M.: "Changes of near-UV CD spectrum of human hemoglobin upon oxygen binding"Biospectroscopy. (In press).

    • Related Report
      2003 Annual Research Report
  • [Publications] Okishio, N., Tanaka, N., Fukuda, R., Nagai, M.: "Differential ligand recognition by Src and PI3K Src homology 3 domeinsC CD and UV resonance Raman studies"Biochemistry. 42・1. 208-216 (2003)

    • Related Report
      2003 Annual Research Report
  • [Publications] Nagatomo S., Jin, Y., Nagai M., Hori, H., Kitagawa, T.: "Changes in the abnormal α-subunit upon CO binding to the normal β-subunit of Hemoglobin M Boston"Biophysical Chemistry. 98. 217-232 (2002)

    • Related Report
      2003 Annual Research Report
  • [Publications] Nagatomo S., Nagai M., Shibayama, N., Kitagawa, T.: "Differences in changes of the α1β2 subunit contacts between ligand binding to the α and β subunits of Hemoglobin A"Biochemistry. 41・31. 10010-10020 (2002)

    • Related Report
      2003 Annual Research Report
  • [Publications] Nagatomo, S., Jin, Y., Nagai, M., Hori, H., Kitagawa, T.: "Changes in the abnormal α-subunit upon CO-binding to the normal β-subunit of Hb M Boston : resonance Raman, EPR, and CD study"Biophys.J.. 98. 217-232 (2002)

    • Related Report
      2002 Annual Research Report
  • [Publications] Nagatomo, S., Nagai, M., Shibayama, N., Kitagawa, T.: "Differences in changes of the α1β2 subunit contacts between ligand binding to the α and β subunits of Hb A : UV resonance Raman analysis using Ni-Fe hybrid hemoglobin"Biochemistry. 41(21). 10010-10020 (2002)

    • Related Report
      2002 Annual Research Report
  • [Publications] Okishio, N., Tanaka, T., Fukuda, R., Nagai, M.: "Differential ligand recognition by the Src and phosphatidylinositol 3-kinase Src SH3 domeins : Circular dichroism and ultraviolet resonance Raman studies"Biochemistry. 42(2). 208-216 (2003)

    • Related Report
      2002 Annual Research Report

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Published: 2002-04-01   Modified: 2016-04-21  

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