1MEK
HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 40 STRUCTURES
Summary for 1MEK
| Entry DOI | 10.2210/pdb1mek/pdb |
| Descriptor | PROTEIN DISULFIDE ISOMERASE (1 entity in total) |
| Functional Keywords | electron transport, redox-active center, isomerase, endoplasmic reticulum |
| Biological source | Homo sapiens (human) |
| Cellular location | Endoplasmic reticulum lumen: P07237 |
| Total number of polymer chains | 1 |
| Total formula weight | 13276.91 |
| Authors | Kemmink, J.,Darby, N.J.,Dijkstra, K.,Nilges, M.,Creighton, T.E. (deposition date: 1996-04-16, release date: 1997-04-21, Last modification date: 2024-10-16) |
| Primary citation | Kemmink, J.,Darby, N.J.,Dijkstra, K.,Nilges, M.,Creighton, T.E. Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. Biochemistry, 35:7684-7691, 1996 Cited by PubMed Abstract: As a first step in dissecting the structure of human protein disulfide isomerase (PDI), the structure of a fragment corresponding to the first 120 residues of its sequence has been determined using heteronuclear multidimensional NMR techniques. As expected from its primary structure homology, the fragment has the thioredoxin fold. Similarities and differences in their structures help to explain why thioredoxins are reductants, whereas PDI is an oxidant of protein thiol groups. The results confirm that PDI has a modular, multidomain structure, which will facilitate its structural and functional characterization. PubMed: 8672469DOI: 10.1021/bi960335m PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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