Modeling of Human Neuraminidase-1 and Its Validation by LERE-Correlation Analysis

DOI Web Site 44 References Open Access
  • Hitaoka Seiji
    Institute of Health Biosciences, The University of Tokushima Graduate School
  • Shibata Yuto
    Institute of Health Biosciences, The University of Tokushima Graduate School
  • Matoba Hiroshi
    Institute of Health Biosciences, The University of Tokushima Graduate School
  • Kawano Akihiro
    Institute of Health Biosciences, The University of Tokushima Graduate School
  • Harada Masataka
    Institute of Health Biosciences, The University of Tokushima Graduate School
  • Rahman M Motiur
    Institute of Health Biosciences, The University of Tokushima Graduate School
  • Tsuji Daisuke
    Institute of Health Biosciences, The University of Tokushima Graduate School
  • Hirokawa Takatsugu
    Computational Biology Research Center (CBRC), National Institute of Advanced Industrial Science and Technology (AIST)
  • Itoh Kohji
    Institute of Health Biosciences, The University of Tokushima Graduate School
  • Yoshida Tatsusada
    Institute of Health Biosciences, The University of Tokushima Graduate School
  • Chuman Hiroshi
    Institute of Health Biosciences, The University of Tokushima Graduate School

Bibliographic Information

Other Title
  • ヒト・ノイラミニダーゼ-1の立体構造予測と代表エネルギー項を用いた自由エネルギー変化の線形表現解析法によるその検証

Description

Four human neuraminidases (hNEUs1-4) have been identified. Among them, hNEU1 has been studied extensively as a target for sialidosis. It has been desired to understand the biological functions of hNEU1 at the molecular and atomic levels. The three-dimensional structure of hNEU1 is not known at present. In the present work, we constructed a three-dimensional structure of hNEU1 by homology modeling, and then performed correlation analyses between observed and calculated free-energy changes (quantitative structure−activity relationship (QSAR) analyses), coupled with LERE (linear expression by representative energy terms) procedure using the modeled three-dimensional structure in order to confirm the validity of the modeled structure. The atomic coordinates of all atoms in the verified model of hNEU1 are available. The proposed structure of hNEU1 will be useful and helpful for further studies concerning the biological and chemical functions of hNEU1. The present article is one of continuous works derived from the one that won the CBI Award for the best presentation in the CBI/JSBi 2011 Joint Conference (presented by Seiji Hitaoka).

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