1MDI

HIGH RESOLUTION SOLUTION NMR STRUCTURE OF MIXED DISULFIDE INTERMEDIATE BETWEEN MUTANT HUMAN THIOREDOXIN AND A 13 RESIDUE PEPTIDE COMPRISING ITS TARGET SITE IN HUMAN NFKB

1MDI の概要

• エントリーDOI: 10.2210/pdb1mdi/pdb
• 分子名称: THIOREDOXIN, TARGET SITE IN HUMAN NFKB (3 entities in total)
• 機能のキーワード: complex (electron transport-peptide), complex (electron transport-peptide) complex, complex (electron transport/peptide)
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P10599 P19838
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13149.88

構造登録者

Clore, G.M.,Qin, J.,Gronenborn, A.M. (登録日: 1995-02-27, 公開日: 1995-06-03, 最終更新日: 2024-10-16)

主引用文献

Qin, J.,Clore, G.M.,Kennedy, W.M.,Huth, J.R.,Gronenborn, A.M.
Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B.
Structure, 3:289-297, 1995

PubMed Abstract: Human thioredoxin is a 12 kDa cellular redox protein that plays a key role in maintaining the redox environment of the cell. It has recently been shown to be responsible for activating the DNA-binding properties of the cellular transcription factor, NF kappa B, by reducing a disulfide bond involving Cys62 of the p50 subunit. Using multidimensional heteronuclear-edited and hetero-nuclear-filtered NMR spectroscopy, we have solved the solution structure of a complex of human thioredoxin and a 13-residue peptide extending from residues 56-68 of p50, representing a kinetically stable mixed disulfide intermediate along the reaction pathway.

PubMed: 7788295
DOI: 10.1016/S0969-2126(01)00159-9

実験手法

SOLUTION NMR