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

收藏

页码：377 / 382

页数：6

相关论文

共 50 条

[41] ON THE PREPARATION AND X-RAY DATA-COLLECTION OF ISOMORPHOUS XENON DERIVATIVES [J].

SCHILTZ, M ;

PRANGE, T ;

FOURME, R .

JOURNAL OF APPLIED CRYSTALLOGRAPHY, 1994, 27 (pt 6) :950-960

[42] THE CRYSTAL-STRUCTURE OF THE ESTROGEN-RECEPTOR DNA-BINDING DOMAIN BOUND TO DNA - HOW RECEPTORS DISCRIMINATE BETWEEN THEIR RESPONSE ELEMENTS [J].

SCHWABE, JWR ;

CHAPMAN, L ;

FINCH, JT ;

RHODES, D .

CELL, 1993, 75 (03) :567-578

[43]

STROMSTEDT PE, 1990, J BIOL CHEM, V265, P12973

[44] DISTINCT CLASSES OF TRANSCRIPTIONAL ACTIVATING DOMAINS FUNCTION BY DIFFERENT MECHANISMS [J].

TASSET, D ;

TORA, L ;

FROMENTAL, C ;

SCHEER, E ;

CHAMBON, P .

CELL, 1990, 62 (06) :1177-1187

[45] A MUTATION IN THE LIGAND-BINDING DOMAIN OF THE ANDROGEN RECEPTOR OF HUMAN LNCAP CELLS AFFECTS STEROID BINDING CHARACTERISTICS AND RESPONSE TO ANTI-ANDROGENS [J].

VELDSCHOLTE, J ;

RISSTALPERS, C ;

KUIPER, GGJM ;

JENSTER, G ;

BERREVOETS, C ;

CLAASSEN, E ;

VANROOIJ, HCJ ;

TRAPMAN, J ;

BRINKMANN, AO ;

MULDER, E .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1990, 173 (02) :534-540

[46]

WRENN CK, 1993, J BIOL CHEM, V268, P24089

[47] DROSOPHILA ULTRASPIRACLE MODULATES ECDYSONE RECEPTOR FUNCTION VIA HETERODIMER FORMATION [J].

YAO, TP ;

SEGRAVES, WA ;

ORO, AE ;

MCKEOWN, M ;

EVANS, RM .

CELL, 1992, 71 (01) :63-72

[48] THE DIMERIZATION INTERFACES FORMED BETWEEN THE DNA-BINDING DOMAINS OF RXR, RAR AND TR DETERMINE THE BINDING-SPECIFICITY AND POLARITY OF THE FULL-LENGTH RECEPTORS TO DIRECT REPEATS [J].

ZECHEL, C ;

SHEN, XQ ;

CHEN, JY ;

CHEN, ZP ;

CHAMBON, P ;

GRONEMEYER, H .

EMBO JOURNAL, 1994, 13 (06) :1425-1433

[49] V-ERBA ONCOGENE ACTIVATION ENTAILS THE LOSS OF HORMONE-DEPENDENT REGULATOR ACTIVITY OF C-ERBA [J].

ZENKE, M ;

MUNOZ, A ;

SAP, J ;

VENNSTROM, B ;

BEUG, H .

CELL, 1990, 61 (06) :1035-1049

[50] MUTATIONS THAT ALTER LIGAND-INDUCED SWITCHES AND DIMERIZATION ACTIVITIES IN THE RETINOID-X RECEPTOR [J].

ZHANG, XK ;

SALBERT, G ;

LEE, MO ;

PFAHL, M .

MOLECULAR AND CELLULAR BIOLOGY, 1994, 14 (06) :4311-4323

← 1 2 3 4 5 →