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1CQG

HIGH RESOLUTION SOLUTION NMR STRUCTURE OF MIXED DISULFIDE INTERMEDIATE BETWEEN HUMAN THIOREDOXIN (C35A, C62A, C69A, C73A) MUTANT AND A 13 RESIDUE PEPTIDE COMPRISING ITS TARGET SITE IN HUMAN REF-1 (RESIDUES 59-71 OF THE P50 SUBUNIT OF NFKB), NMR, 31 STRUCTURES

1CQG の概要
エントリーDOI10.2210/pdb1cqg/pdb
関連するPDBエントリー1CQH
分子名称THIOREDOXIN, REF-1 PEPTIDE (2 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
Nucleus. DNA-(apurinic or apyrimidinic site) lyase, mitochondrial: Mitochondrion: P27695
タンパク質・核酸の鎖数2
化学式量合計12996.74
構造登録者
Clore, G.M.,Qin, J.,Gronenborn, A.M. (登録日: 1996-04-02, 公開日: 1996-08-01, 最終更新日: 2024-10-16)
主引用文献Qin, J.,Clore, G.M.,Kennedy, W.P.,Kuszewski, J.,Gronenborn, A.M.
The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal.
Structure, 4:613-620, 1996
Cited by
PubMed Abstract: Human thioredoxin (hTRX) is a 12 kDa cellular redox protein that has been shown to play an important role in the activation of a number of transcriptional and translational regulators via a thiol-redox mechanism. This activity may be direct or indirect via another redox protein known as Ref-1. The structure of a complex of hTRX with a peptide comprising its target from the transcription factor NF kappa B has previously been solved. To further extend our knowledge of the recognition by and interaction of hTRX with its various targets, we have studied a complex between hTRX and a Ref-1 peptide. This complex represents a kinetically stable mixed disulfide intermediate along the reaction pathway.
PubMed: 8736558
DOI: 10.1016/S0969-2126(96)00065-2
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 1cqg
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-29に公開中

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