2RTU

Solution structure of oxidized human HMGB1 A box

2RTU の概要

• エントリーDOI: 10.2210/pdb2rtu/pdb
• NMR情報: BMRB: 11532
• 分子名称: High mobility group protein B1 (1 entity in total)
• 機能のキーワード: disulfide bond, high mobility group box 1, dna binding protein
• 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: 10118.66

構造登録者

Jing, W.,Tochio, N.,Tate, S. (登録日: 2013-09-12, 公開日: 2014-03-05, 最終更新日: 2024-10-30)

主引用文献

Wang, J.,Tochio, N.,Takeuchi, A.,Uewaki, J.,Kobayashi, N.,Tate, S.
Redox-sensitive structural change in the A-domain of HMGB1 and its implication for the binding to cisplatin modified DNA.
Biochem.Biophys.Res.Commun., 441:701-706, 2013

PubMed Abstract: HMGB1 (high-mobility group B1) is a ubiquitously expressed bifunctional protein that acts as a nuclear protein in cells and also as an inflammatory mediator in the extracellular space. HMGB1 changes its functions according to the redox states in both intra- and extra-cellular environments. Two cysteines, Cys23 and Cys45, in the A-domain of HMGB1 form a disulfide bond under oxidative conditions. The A-domain with the disulfide bond shows reduced affinity to cisplatin modified DNA. We have solved the oxidized A-domain structure by NMR. In the structure, Phe38 has a flipped ring orientation from that found in the reduced form; the phenyl ring in the reduced form intercalates into the platinated lesion in DNA. The phenyl ring orientation in the oxidized form is stabilized through intramolecular hydrophobic contacts. The reorientation of the Phe38 ring by the disulfide bond in the A-domain may explain the reduced HMGB1 binding affinity towards cisplatinated DNA.

PubMed: 24427810

実験手法

SOLUTION NMR