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2013 Fiscal Year Final Research Report

Elucidation of the mechanism of the specific interaction of a mouse peptide pheromone ESP1 and the class-C GPCR receptor

Research Project

  • PDF
Project/Area Number 24780104
Research Category

Grant-in-Aid for Young Scientists (B)

Allocation TypeMulti-year Fund
Research Field Applied biochemistry
Research InstitutionKumamoto University

Principal Investigator

YOSHINAGA Sosuke  熊本大学, 生命科学研究部, 助教 (00448515)

Research Collaborator TOUHARA Kazushige  東京大学, 大学院農学生命科学研究科, 教授 (00280925)
Project Period (FY) 2012-04-01 – 2014-03-31
Keywords情報伝達 / フェロモン / NMR / 立体構造 / 相互作用 / マウス / GPCR / ぺプチド
Research Abstract

Animals communicate using "pheromones", which are tools for accurate recognition of the opposite sex, to preserve the species. Our collaborators, the Touhara group at the University of Tokyo, identified ESP1, which is a peptidic sex pheromone that is released in male mouse tear fluids and enhances female sexual receptive behavior (Nature, 2005). They also elucidated that ESP1 is selectively recognized by a specific class-C G-protein-coupled receptor (GPCR), V2Rp5, which is expressed in the vomeronasal organ that is located beneath the nasal septum (Nature, 2010).
We determined the three dimensional structure of ESP1, and revealed the binding mode between ESP1 and the receptor V2Rp5, based on these structures (JBC, 2013). To our knowledge, this is the first report of the structural information about the interaction between a mammalian peptide pheromone and its receptor.

  • Research Products

    (5 results)

All 2014 2013 Other

All Journal Article (4 results) (of which Peer Reviewed: 4 results) Remarks (1 results)

  • [Journal Article] Expression and purification of mouse peptide ESP4 in Escherichia coli2014

    • Author(s)
      Hirakane, M., Taniguchi, M., Yoshinaga, S., Misumi, S., and Terasawa, H.
    • Journal Title

      Protein Expression and Purification

      Volume: 96 Pages: 20–25

    • DOI

      10.1016/j.pep.2014.01.010

    • Peer Reviewed
  • [Journal Article] Backbone and side-chain ^1 H, ^<15> N and ^<13>C assignments of mouse peptide ESP42014

    • Author(s)
      Taniguchi, M., Yoshinaga, S., Haga-Yamanaka, H., Touhara, K., and Terasawa, H.
    • Journal Title

      Biomolecular NMR Assignments

      Volume: 8 Pages: 7–9

    • DOI

      10.1007/s12104-012-9441-7

    • Peer Reviewed
  • [Journal Article] マウスの性行動を制御するペプチド性フェロモンESP1の立体構造決定―クラスCタイプGPCRによるリガンド認識機構の解析―2014

    • Author(s)
      谷口雅浩,吉永壮佐,佐藤徹,はが紗智子,東原和成,寺沢宏明
    • Journal Title

      化学と生物

      Volume: 52 Pages: 67–69

    • Peer Reviewed
  • [Journal Article] Structure of the mouse sex peptide pheromone ESP1 reveals a molecular basis for specific binding to the class C G-protein-coupled vomeronasal receptor2013

    • Author(s)
      Yoshinaga, S., Sato, T., Hirakane, M., Esaki, K., Hamaguchi, T., Haga-Yamanaka, S., Tsunoda, M., Kimoto, H., Shimada, I., Touhara, K., and Terasawa, H.
    • Journal Title

      Journal of Biological Chemistry

      Volume: 288 Pages: 16064–16072

    • DOI

      10.1074/jbc.M112.436782

    • Peer Reviewed
  • [Remarks] 研究成果の紹介「マウスの性行動を制御するペプチド性フェロモンの立体構造と受容体相互作用機構を解明」

    • URL

      http://www.a.u-tokyo.ac.jp/topics/2013/20130509-4.html

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Published: 2015-06-25  

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