Ligand-protein interactions in nuclear receptors of hormones

被引:88
作者
Egea, PF [1 ]
Klaholz, BP [1 ]
Moras, D [1 ]
机构
[1] ULP, CNRS,INSERM, Inst Genet & Biol Mol & Cellulaire, Lab Biol & Genom Struct, F-67404 Illkirch, France
关键词
nuclear receptor; ligand binding domain; transcriptional regulation; ligand-protein interaction; selectivity; molecular recognition;
D O I
10.1016/S0014-5793(00)01672-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Nuclear hormone receptors are transcription factors regulated by lipophilic ligands, These hormones bind to their nuclear receptor targets using an induced fit mechanism that triggers a large conformational change and generates the proper surface for the binding of protein coactivators. The molecular details of the various steps of this activation process or its inhibition by antagonists are now understood for several nuclear receptors, (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V, All rights reserved.
引用
收藏
页码:62 / 67
页数:6
相关论文
共 49 条
[1]  
ALLEGRETTO EA, 1993, J BIOL CHEM, V268, P26625
[2]   RETINOIC ACID RECEPTORS AND RETINOID X-RECEPTORS - INTERACTIONS WITH ENDOGENOUS RETINOIC ACIDS [J].
ALLENBY, G ;
BOCQUEL, MT ;
SAUNDERS, M ;
KAZMER, S ;
SPECK, J ;
ROSENBERGER, M ;
LOVEY, A ;
KASTNER, P ;
GRIPPO, JF ;
CHAMBON, P ;
LEVIN, AA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (01) :30-34
[3]   Retinoic acid receptor: A simulation analysis of retinoic acid binding and the resulting conformational changes [J].
Blondel, A ;
Renaud, JP ;
Fischer, S ;
Moras, D ;
Karplus, M .
JOURNAL OF MOLECULAR BIOLOGY, 1999, 291 (01) :101-115
[4]   Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains [J].
Bourguet, W ;
Vivat, V ;
Wurtz, JM ;
Chambon, P ;
Gronemeyer, H ;
Moras, D .
MOLECULAR CELL, 2000, 5 (02) :289-298
[5]   CRYSTAL-STRUCTURE OF THE LIGAND-BINDING DOMAIN OF THE HUMAN NUCLEAR RECEPTOR RXR-ALPHA [J].
BOURGUET, W ;
RUFF, M ;
CHAMBON, P ;
GRONEMEYER, H ;
MORAS, D .
NATURE, 1995, 375 (6530) :377-382
[6]   Molecular basis of agonism and antagonism in the oestrogen receptor [J].
Brzozowski, AM ;
Pike, ACW ;
Dauter, Z ;
Hubbard, RE ;
Bonn, T ;
Engstrom, O ;
Ohman, L ;
Greene, GL ;
Gustafsson, JA ;
Carlquist, M .
NATURE, 1997, 389 (6652) :753-758
[7]   A decade of molecular biology of retinoic acid receptors [J].
Chambon, P .
FASEB JOURNAL, 1996, 10 (09) :940-954
[8]   Structure and specificity of nuclear receptor-coactivator interactions [J].
Darimont, BD ;
Wagner, RL ;
Apriletti, JW ;
Stallcup, MR ;
Kushner, PJ ;
Baxter, JD ;
Fletterick, RJ ;
Yamamoto, KR .
GENES & DEVELOPMENT, 1998, 12 (21) :3343-3356
[9]   Crystal structure of the human RXRα ligand-binding domain bound to its natural ligand:: 9-cis retinoic acid [J].
Egea, PF ;
Mitschler, A ;
Rochel, N ;
Ruff, M ;
Chambon, P ;
Moras, D .
EMBO JOURNAL, 2000, 19 (11) :2592-2601
[10]   Increasing the complexity of coactivation in nuclear receptor signaling [J].
Freedman, LP .
CELL, 1999, 97 (01) :5-8