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Nuclear magnetic resonance characterization of the N‐terminal thioredoxin‐like domain of protein disulfide isomerase
Author(s) -
Kemmink Johan,
Darby Nigel J.,
Creighton Thomas E.,
Dijkstra Klaas,
Scheek Ruud M.
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560041216
Subject(s) - protein disulfide isomerase , ferredoxin thioredoxin reductase , terminal (telecommunication) , thioredoxin , chemistry , characterization (materials science) , isomerase , protein folding , disulfide bond , posttranslational modification , nuclear magnetic resonance , resonance (particle physics) , biochemistry , biophysics , physics , enzyme , biology , nanotechnology , materials science , computer science , thioredoxin reductase , telecommunications , particle physics
A genetically engineered protein consisting of the 120 residues at the N‐terminus of human protein disulfide isomerase (PDI) has been characterized by 1 H, 13 C, and 15 N NMR methods. The sequence of this protein is 35% identical to Escherichia coli thioredoxin, and it has been found also to have similar patterns of secondary structure and β ‐sheet topology. The results confirm that PDI is a modular, multidomain protein. The last 20 residues of the N‐terminal domain of PDI are some of those that are similar to part of the estrogen receptor, yet they appear to be an intrinsic part of the thioredoxin fold. This observation makes it unlikely that any of the segments of PDI with similarities to the estrogen receptor comprise individual domains.