1JUN

NMR STUDY OF C-JUN HOMODIMER

1JUN の概要

• エントリーDOI: 10.2210/pdb1jun/pdb
• 分子名称: C-JUN HOMODIMER (1 entity in total)
• 機能のキーワード: transcription regulation, dna-binding regulatory protein, oncogene protein, transcription activation
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P05412
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 9767.43

構造登録者

Junius, F.K.,O'Donoghue, S.I.,Nilges, M.,King, G.F. (登録日: 1995-12-19, 公開日: 1996-06-20, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

SOLUTION NMR