Structural role of a detergent molecule in retinoic acid nuclear receptor crystals

被引：13

作者：

Klaholz, BP ^{[1
]}

Moras, D ^{[1
]}

机构：

[1] ULP, CNRS,INSERM, Inst Genet & Biol Mol & Cellulaire, Struct Biol Lab, F-67404 Illkirch, France

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2000年 / 56卷

关键词：

D O I：

10.1107/S090744490000634X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The human nuclear receptor of retinoic acid hRAR gamma is a ligand-dependent transcription regulator. The presence of a completely ordered dodecyl-alpha-D-maltoside molecule in the crystal structure of the hRAR gamma ligand-binding domain (LBD) refined at 1.3 Angstrom resolution is reported. The non-ionic detergent is required for stabilization and crystallization of the hRAR gamma 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.

引用

页码：933 / 935

页数：3

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