High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer

被引:84
作者
Junius, FK
ODonoghue, SI
Nilges, M
Weiss, AS
King, GF
机构
[1] UNIV SYDNEY,DEPT BIOCHEM,SYDNEY,NSW 2006,AUSTRALIA
[2] EUROPEAN MOLEC BIOL LAB,D-69012 HEIDELBERG,GERMANY
关键词
D O I
10.1074/jbc.271.23.13663
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
The solution structure of the c-Jun leucine zipper domain has been determined to high resolution using a new calculation protocol designed to handle highly ambiguous sets of interproton distance restraints, The domain comprises a coiled coil of parallel alpha-helices in which most of the hydrophobic residues are buried at the highly symmetrical dimer interface; this Interface extends over 10 helical turns and is the most elongated protein domain solved to date using MMR methods, The backbone fold is very similar to that seen in crystal structures of the GCN4 and Jun-Fos leucine zippers; however, in contrast with these crystal structures, the Jun leucine zipper dimer appears to be devoid of favorable intermolecular electrostatic interactions, A polar asparagine residue, located at the dimer interface, forms the sole point of asymmetry in the structure; furthermore, the side chain of this residue is disordered due to motional averaging, This residue, which is highly conserved in the leucine zipper family of transcription factors, provides a destabilizing influence that is likely to facilitate the rapid exchange of zipper strands in vivo.
引用
收藏
页码:13663 / 13667
页数:5
相关论文
共 39 条
[1]  
[Anonymous], FOS JUN FAMILIES TRA
[2]   A FAST ALGORITHM FOR RENDERING SPACE-FILLING MOLECULE PICTURES [J].
BACON, D ;
ANDERSON, WF .
JOURNAL OF MOLECULAR GRAPHICS, 1988, 6 (04) :219-220
[3]   CHARACTERIZATION OF ATOMIC RESOLUTION OF PEPTIDE HELICAL STRUCTURES [J].
BENEDETTI, E ;
DIBLASIO, B ;
PAVONE, V ;
PEDONE, C ;
TONIOLO, C ;
CRISMA, M .
BIOPOLYMERS, 1992, 32 (04) :453-456
[4]   COILED-COIL REGIONS IN THE CARBOXY-TERMINAL DOMAINS OF DYSTROPHIN AND RELATED PROTEINS - POTENTIALS FOR PROTEIN-PROTEIN INTERACTIONS [J].
BLAKE, DJ ;
TINSLEY, JM ;
DAVIES, KE ;
KNIGHT, AE ;
WINDER, SJ ;
KENDRICKJONES, J .
TRENDS IN BIOCHEMICAL SCIENCES, 1995, 20 (04) :133-135
[5]  
BRUNGER AT, 1993, XPLOR USER MANUAL VE
[6]   OBSERVATION OF INTER-SUBUNIT NUCLEAR OVERHAUSER EFFECTS IN A DIMERIC PROTEIN - APPLICATION TO THE ARC REPRESSOR [J].
BURGERING, MJM ;
BOELENS, R ;
CAFFREY, M ;
BREG, JN ;
KAPTEIN, R .
FEBS LETTERS, 1993, 330 (01) :105-109
[7]   THE PACKING OF ALPHA-HELICES - SIMPLE COILED-COILS [J].
CRICK, FHC .
ACTA CRYSTALLOGRAPHICA, 1953, 6 (8-9) :689-697
[8]   THE GCN4 BASIC REGION LEUCINE ZIPPER BINDS DNA AS A DIMER OF UNINTERRUPTED ALPHA-HELICES - CRYSTAL-STRUCTURE OF THE PROTEIN-DNA COMPLEX [J].
ELLENBERGER, TE ;
BRANDL, CJ ;
STRUHL, K ;
HARRISON, SC .
CELL, 1992, 71 (07) :1223-1237
[9]   RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN [J].
FERREDAMARE, AR ;
PRENDERGAST, GC ;
ZIFF, EB ;
BURLEY, SK .
NATURE, 1993, 363 (6424) :38-45
[10]   CRYSTAL-STRUCTURE OF THE HETERODIMERIC BZIP TRANSCRIPTION FACTOR C-FOS-C-JUN BOUND TO DNA [J].
GLOVER, JNM ;
HARRISON, SC .
NATURE, 1995, 373 (6511) :257-261