エンケファリンの立体構造に基づくμ/δ-オピオイドレセプターの基質特異性
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概要
- 論文の詳細を見る
Enkephalin is a morphine-like pentapeptide : Tyr-Gly-Gly-Phe-Xxx, Xxx = Met or Leu. To consider the relationship between the enkephalin conformation and the opioid receptor, the crystal structures of enkephalin analogues were analyzed by the X-ray diffraction method, and two characteristic forms were observed as the fundamental conformation of enkephalin, One is the β -turn structure and the other the antiparallelly extended dimer (ED) structure. From the NMR and CD spectral studies, it was suggested that the β -turn and ED structures of enkephalin are the most probable conformations for the binding to μ -and δ -receptors, respectively. Further, the molecular-dynamics simulations indicated that these conformation are both advantageous in energetical term. Based on the insight of the enkephalin conformation, it was attempted to convert the μ -selective morphine toward δ -affinitive ligand by the dimerization.
- 日本生物物理学会の論文
- 1990-05-25
著者
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土井 光暢
大阪薬大
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石田 寿昌
大阪薬大
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土井 光暢
大阪薬科大学
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石田 寿昌
大阪薬科大学
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土井 充暢
Osaka University of Pharmaceutical Sciences
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石田 寿晶
大阪薬科大学
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Doi Mitsunobu
Department Of Physical Chemistry Osaka University Of Pharmaceutical Sciences
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