1OLH

HIGH-RESOLUTION SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR

1OLH の概要

• エントリーDOI: 10.2210/pdb1olh/pdb
• 分子名称: TUMOR SUPPRESSOR P53 (OLIGOMERIZATION DOMAIN) (1 entity in total)
• 機能のキーワード: anti-oncogene protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm. Isoform 1: Nucleus. Isoform 2: Nucleus. Isoform 3: Nucleus. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 8: Nucleus. Isoform 9: Cytoplasm: P04637
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 19794.53

構造登録者

Clore, G.M.,Omichinski, J.G.,Gronenborn, A.M. (登録日: 1994-06-13, 公開日: 1995-03-31, 最終更新日: 2024-05-22)

主引用文献

Clore, G.M.,Omichinski, J.G.,Sakaguchi, K.,Zambrano, N.,Sakamoto, H.,Appella, E.,Gronenborn, A.M.
High-resolution structure of the oligomerization domain of p53 by multidimensional NMR.
Science, 265:386-391, 1994

PubMed Abstract: The three-dimensional structure of the oligomerization domain (residues 319 to 360) of the tumor suppressor p53 has been solved by multidimensional heteronuclear magnetic resonance (NMR) spectroscopy. The domain forms a 20-kilodalton symmetric tetramer with a topology made up from a dimer of dimers. The two primary dimers each comprise two antiparallel helices linked by an antiparallel beta sheet. One beta strand and one helix are contributed from each monomer. The interface between the two dimers forming the tetramer is mediated solely by helix-helix contacts. The overall result is a symmetric, four-helix bundle with adjacent helices oriented antiparallel to each other and with the two antiparallel beta sheets located on opposing faces of the molecule. The tetramer is stabilized not only by hydrophobic interactions within the protein core but also by a number of electrostatic interactions. The implications of the structure of the tetramer for the biological function of p53 are discussed.

PubMed: 8023159

実験手法

SOLUTION NMR