CRYSTAL-STRUCTURE OF THE LIGAND-BINDING DOMAIN OF THE HUMAN NUCLEAR RECEPTOR RXR-ALPHA

被引：1002

作者：

BOURGUET, W ^{[1
]}

RUFF, M ^{[1
]}

CHAMBON, P ^{[1
]}

GRONEMEYER, H ^{[1
]}

MORAS, D ^{[1
]}

机构：

[1] UNIV STRASBOURG 1,COLL FRANCE,INST GENET & BIOL MOLEC & CELLULAIRE,CNRS,INSERM,F-67404 ILLKIRCH GRAFFENS,FRANCE

来源：

NATURE | 1995年 / 375卷 / 6530期

关键词：

D O I：

10.1038/375377a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The crystal structure of the human retinoid-X receptor RXR-alpha ligand-binding domain reveals a previously undiscovered fold of an antiparallel alpha-helical sandwich, packed as dimeric units. Two helices and one loop form the homodimerization surface, and hydrophobic heptad repeats participate in stabilizing the fold. The existence of a ligand-binding pocket is proposed that would allow 9-cis retinoic acid to interact with different functional modules, including the AF-2 activating domain. Several lines of evidence indicate that the overall structure is a prototype fold of ligand-binding domains of nuclear receptors.

引用

页码：377 / 382

页数：6

共 50 条

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AMEZ JG, 1994, J APPL CRYSTALLOGR, V27, P649

[2]

[Anonymous], 1994, ACTA CRYSTALLOGR D, V50, P760

[3] THE CONSERVED 9TH C-TERMINAL HEPTAD IN THYROID-HORMONE AND RETINOIC ACID RECEPTORS MEDIATES DIVERSE RESPONSES BY AFFECTING HETERODIMER BUT NOT HOMODIMER FORMATION [J].