1ERT
HUMAN THIOREDOXIN (REDUCED FORM)
Summary for 1ERT
Entry DOI | 10.2210/pdb1ert/pdb |
Descriptor | THIOREDOXIN (2 entities in total) |
Functional Keywords | dimer, thioredoxin, oxidoreductase |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus : P10599 |
Total number of polymer chains | 1 |
Total formula weight | 11750.48 |
Authors | Weichsel, A.,Gasdaska, J.R.,Powis, G.,Montfort, W.R. (deposition date: 1996-02-07, release date: 1996-10-14, Last modification date: 2024-10-16) |
Primary citation | Weichsel, A.,Gasdaska, J.R.,Powis, G.,Montfort, W.R. Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure, 4:735-751, 1996 Cited by PubMed Abstract: Human thioredoxin reduces the disulfide bonds of numerous proteins in vitro, and can activate transcription factors such as NFkB in vivo. Thioredoxin can also act as a growth factor, and is overexpressed and secreted in certain tumor cells. PubMed: 8805557DOI: 10.1016/S0969-2126(96)00079-2 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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