2KG4

Three-dimensional structure of human Gadd45alpha in solution by NMR

2KG4 の概要

• エントリーDOI: 10.2210/pdb2kg4/pdb
• NMR情報: BMRB: 15855
• 分子名称: Growth arrest and DNA-damage-inducible protein GADD45 alpha (1 entity in total)
• 機能のキーワード: gadd45, growth arrest, dna damage, flexible regions, monomer, cell cycle
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18351.72

構造登録者

Sanchez, R.,Pantoja-Uceda, D.,Prieto, J.,Diercks, T.,Campos-Olivas, R.,Blanco, F.J. (登録日: 2009-03-04, 公開日: 2009-03-31, 最終更新日: 2024-05-15)

主引用文献

Sanchez, R.,Pantoja-Uceda, D.,Prieto, J.,Diercks, T.,Marcaida, M.J.,Montoya, G.,Campos-Olivas, R.,Blanco, F.J.
Solution structure of human growth arrest and DNA damage 45alpha (Gadd45alpha) and its interactions with proliferating cell nuclear antigen (PCNA) and Aurora A kinase
J.Biol.Chem., 285:22196-22201, 2010

PubMed Abstract: Gadd45alpha is a nuclear protein encoded by a DNA damage-inducible gene. Through its interactions with other proteins, Gadd45alpha participates in the regulation of DNA repair, cell cycle, cell proliferation, and apoptosis. The NMR structure of human Gadd45alpha has been determined and shows an alpha/beta fold with two long disordered and flexible regions at the N terminus and one of the loops. Human Gadd45alpha is predominantly monomeric in solution but exists in equilibrium with dimers and other oligomers whose population increases with protein concentration. NMR analysis shows that Aurora A interacts through its N-terminal domain with a region of human Gadd45alpha encompassing the site of dimerization, suggesting that the oligomerization of Gadd45alpha could be a regulatory mechanism to modulate its interactions with Aurora A, and possibly with other proteins too. However, Gadd45alpha appears to interact only weakly with PCNA through its flexible loop, in contrast with previous and contradictory reports.

PubMed: 20460379
DOI: 10.1074/jbc.M109.069344

実験手法

SOLUTION NMR