1JUN

NMR STUDY OF C-JUN HOMODIMER

Summary for 1JUN

• Entry DOI: 10.2210/pdb1jun/pdb
• Descriptor: C-JUN HOMODIMER (1 entity in total)
• Functional Keywords: transcription regulation, dna-binding regulatory protein, oncogene protein, transcription activation
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P05412
• Total number of polymer chains: 2
• Total formula weight: 9767.43

Authors

Junius, F.K.,O'Donoghue, S.I.,Nilges, M.,King, G.F. (deposition date: 1995-12-19, release date: 1996-06-20, Last modification date: 2024-10-23)

Primary citation

Junius, F.K.,O'Donoghue, S.I.,Nilges, M.,Weiss, A.S.,King, G.F.
High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer.
J.Biol.Chem., 271:13663-13667, 1996

PubMed 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.

PubMed: 8662824
DOI: 10.1074/jbc.271.23.13663

Experimental method

SOLUTION NMR