1MDJ
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 NFKB (RESIDUES 56-68 OF THE P50 SUBUNIT OF NFKB)
Summary for 1MDJ
| Entry DOI | 10.2210/pdb1mdj/pdb |
| Descriptor | THIOREDOXIN, TARGET SITE IN HUMAN NFKB (3 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 P19838 |
| Total number of polymer chains | 2 |
| Total formula weight | 13149.88 |
| Authors | Clore, G.M.,Qin, J.,Gronenborn, A.M. (deposition date: 1995-02-27, release date: 1995-06-03, Last modification date: 2024-10-16) |
| Primary citation | 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 Cited by 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: 7788295DOI: 10.1016/S0969-2126(01)00159-9 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
