PDBsum entry: 1jun

Transcription regulation

PDB id: 1jun

Contents

Protein chains

44 a.a. *

* Residue conservation analysis

PDB id:

1jun

Name:

Transcription regulation

Title:

Nmr study of c-jun homodimer

Structure:

C-jun homodimer. Chain: a, b. Fragment: leucine zipper domain, residues 272 - 315. Synonym: junlz, junp1n. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606

NMR struc:

7 models

Authors:

F.K.Junius,S.I.O'Donoghue,M.Nilges,G.F.King

Key ref:

F.K.Junius et al. (1996). High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer. J Biol Chem, 271, 13663-13667. PubMed id: 8662824 DOI: 10.1074/jbc.271.23.13663

Date:

19-Dec-95 Release date: 20-Jun-96

Protein chains

P05412  (JUN_HUMAN) -  Transcription factor AP-1

Seq: 331 a.a.

Struc: 43 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Cellular component: nucleus (1 term)
• Biological process: regulation of transcription, DNA-dependent (1 term)
• Biochemical function: transcription factor activity (3 terms)

DOI no: 10.1074/jbc.271.23.13663

J Biol Chem 271:13663-13667 (1996)

PubMed id: 8662824

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

F.K.Junius, S.I.O'Donoghue, M.Nilges, A.S.Weiss, G.F.King.

ABSTRACT

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 NMR 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.

Selected figure(s)

Figure 2.
Fig. 2. Solution structure of JunLZ. a, the ensemble of seven refined JunLZ structures superimposed for the best fit over all atoms of the average structure for Leu-280-Leu-308. The side chain heavy atoms are displayed only for those residues at the dimer interface. b, a view down the long axis of the dimer, which highlights the supercoiling of the helices. The median value of the superhelical pitch was calculated (36) to be 137 Å. In a and b, the helix backbones are blue, and the side chains of the d-position Leu residues and the a-position residues, which together form the dimer interface, are red and yellow, respectively. The -carbon atoms are displayed as dark blue spheres in b. b was prepared with the programs MOLSCRIPT Version 1.4 (37) and Raster 3D Version 2.0 (38, 39).

Figure 3.
Fig. 3. Side chain packing at dimer interface of JunLZ. a, a cross-sectional view of JunLZ through the Val-305 residues illustrating that a-position residues pack in a parallel orientation (24), such that a C- -C- bond vector (red) representing the ``knob'' of the interfacial residue lies almost parallel to the C- -C- vector (yellow) at the base of the acceptor hole on the opposing helical strand. b, a cross-sectional view of JunLZ through the Leu-301 residues illustrating that d-position residues pack in a perpendicular orientation (24), such that the C- -C- bond vector is almost perpendicular to the C- -C- vector at the base of the acceptor hole on the opposing helix. In both diagrams, the continuation of the helix backbone on either side of the C- -C- vector is displayed in magenta.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (1996, 271, 13663-13667) copyright 1996.

Figures were selected by an automated process.