1CQH

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, MINIMIZED AVERAGE STRUCTURE

Summary for 1CQH

• Entry DOI: 10.2210/pdb1cqh/pdb
• Related: 1CQG
• Descriptor: THIOREDOXIN, REF-1 PEPTIDE (2 entities in total)
• Functional Keywords: complex, electron transport/peptide, complex (electron transport-peptide) complex, complex (electron transport/peptide)
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P10599; Nucleus. DNA-(apurinic or apyrimidinic site) lyase, mitochondrial: Mitochondrion: P27695
• Total number of polymer chains: 2
• Total formula weight: 12996.74

Authors

Clore, G.M.,Qin, J.,Gronenborn, A.M. (deposition date: 1996-04-02, release date: 1996-08-01, Last modification date: 2024-10-16)

Primary citation

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

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

Experimental method

SOLUTION NMR