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2003 Fiscal Year Final Research Report Summary

The Mechanism of the formation of Reelin complex

Research Project

Project/Area Number 13672318
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Biological pharmacy
Research InstitutionNippon Veterinary and Animal Science University

Principal Investigator

TATE Naoko  Nippon Veterinary and Animal Science University, Veterinary, Associate, 獣医学部, 助教授 (00201955)

Project Period (FY) 2001 – 2003
Keywordsneuron / Reelin / complex / structure
Research Abstract

Reelin is a key molecule of ordered neuronal alignment in the brain. I demonstrated that Rsslin molecules assembled with each other to form a huge protein complex both in vitro and in vivo, which is inhibited by the function-blocking CR-50 antibody (Proc. Natl. Acad. Sci., USA).
In this study, I first showed that the N-terminal 370 amino acids of Reelin that is an epitope against CR-50 antibody played an important role in order to form Reelin-Reelin interaction and this domain consisted of a-helix (20%) and β-sheet (40%) structure. This structure was important for the formation of Reelin complex. Secondary I examined the structure of the F-spondin-like domain which stayed up-stream of CR-50 epitope domain by circular dichroism spectroscopy. The result is that the the F-spondin-like domain had an a-helix (20%) and β-sheet (50%). Then, I analyzed this domain by analitycal gel filtration chromatography. The elution profile showed that the F-spondin-like domain form a homopolymer. Therefore, not only CR-50 epiope but also F-spondin-like domain was thought to contribute to form Reelin complex.
Then, in order to get the information of Reelin molecule structure by nuclear magnetic resonance (NMR) spectroscopy, I explored a new measurement technique of NMR spetroscopy.

  • Research Products

    (2 results)

All Other

All Publications (2 results)

  • [Publications] Kurita, J., Shimahara, H., Tate, N., Tate, S.: "Measurement of ^<15>N chemical shift anisotropy in a protein dissolved in diluted Liquid crystalline medium with the application of magic angle sample spinning."J.Magnetic Resonance. 163. 163-173 (2003)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Kurita, J., Shimahara, H., Tate, N., Tate, S.: "Measurement of ^<15>N chemical shift anisotropy in a protein dissolved in diluted liquid crystalline medium with the application of magic angle sample spinning."J. Magnetic Resonance. 163. 163-173 (2003)

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 2005-04-19  

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