Structure Determination of Drug Target Proteins by Neutron Crystallography

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  • 中性子回折による創薬標的蛋白質の構造解析
  • 中性子回折の基礎と応用(応用12)中性子回折による創薬標的蛋白質の構造解析
  • チュウセイシ カイセツ ノ キソ ト オウヨウ オウヨウ 12 チュウセイシ カイセツ ニ ヨル ソウヤク ヒョウテキ タンパクシツ ノ コウゾウ カイセキ

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Abstract

High resolution X-ray crystallography provides information for most of the atoms comprising the proteins, with the exception of hydrogen atoms. Whereas, neutron crystallography, which is a powerful technique for locating hydrogen atoms, enables us to obtain accurate atomic positions within proteins. Neutron diffraction data can provide information of the location of hydrogen atoms to the structural information determined by X-ray crystallography. Here, we show the recent results 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 0.094nm resolution by X-ray diffraction and 0.165nm resolution by neutron diffraction. The structure of HIV-PR with its potent inhibitor was also determined to 0.093nm resolution by X-ray diffraction and 0.19nm 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 crystallography to identify the location of ambiguous hydrogen atoms will be shown.

Journal

  • RADIOISOTOPES

    RADIOISOTOPES 59 (4), 299-308, 2010

    Japan Radioisotope Association

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