中性子と放射光の相補的な利用による創薬標的タンパク質の立体構造解析  [in Japanese] Collaborative Use of Neutron and X-ray for Determination of Drug Target Proteins  [in Japanese]

Access this Article

Author(s)

Abstract

  Crystallography enables us to obtain accurate atomic positions within proteins. High resolution X-ray crystallography provides information for most of the atoms comprising a protein, with the exception of hydrogens. Neutron diffraction data can provide information of the location of hydrogen atoms, and is complementary to the structural information determined by X-ray crystallography. Here, we show the recent result of the structural determination of drug-target proteins, porcine pancreatic elastase and human immuno-deficiency virus type-1 protease by both X-ray and neutron diffraction. The structure of porcine pancreatic elastase with its potent inhibitor was determined to 0.94 Å resolution by X-ray diffraction and 1.65 Å resolution by neutron diffraction. The structure of HIV-PR with its potent inhibitor was also determined to 0.93 Å resolution by X-ray diffraction and 1.9 Å resolution by neutron diffraction. The ionization state and the location of hydrogen atoms of the catalytic residue in these enzymes were determined by neutron diffraction. Furthermore, collaborative use of both X-ray and neutron to identify the location of ambiguous hydrogen atoms will be shown.<br>

Journal

  • YAKUGAKU ZASSHI

    YAKUGAKU ZASSHI 130(5), 657-664, 2010

    The Pharmaceutical Society of Japan

Codes

  • NII Article ID (NAID)
    130000259451
  • NII NACSIS-CAT ID (NCID)
    AN00284903
  • Text Lang
    JPN
  • ISSN
    0031-6903
  • NDL Article ID
    10697526
  • NDL Source Classification
    ZS51(科学技術--薬学)
  • NDL Call No.
    Z19-411
  • Data Source
    NDL  J-STAGE 
Page Top