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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structural role of a detergent molecule in retinoic acid nuclear receptor crystals
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Structural role of a detergent molecule in retinoic acid nuclear receptor crystals

机译:洗涤剂分子的结构的作用视黄酸核受体的晶体

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摘要

The human nuclear receptor of retinoic acid hRARγ is ligand-dependent transcription regulator. The presence of a completely ordered dodecyl-α-D-maltoside molecule in the crystal structure of the hRARγ ligand-binding domain (LBD) refined at 1.3 A resolution is reported. The non-ionic detergent is required for stabilization and crystallization of the hRARγ LBD and mediates a crystal contact in the region where coactivator proteins bind. Its dodecyl moiety is buried in a hydrophobic channel, whereas the maltoside head group is hydrogen bonded to water molecules and polar residue side chains.
机译:人类的核受体的视黄酸hRARγ是ligand-dependent转录监管机构。存在一个完全有序的十二烷基-α-D-maltoside分子晶体结构的hRARγ配体结合域1.3(小黑裙)精制决议报告。非离子去污剂是必需的稳定的结晶hRARγ小黑裙和调节晶体联系在该地区共激活剂蛋白质绑定。一半埋在疏水性通道,而maltoside头组是氢连着水分子和极地残渣链。

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