Literature DB >> 8580850

Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase.

J Kemmink1, N J Darby, K Dijkstra, R M Scheek, T E Creighton.   

Abstract

A genetically engineered protein consisting of the 120 residues at the N-terminus of human protein disulfide isomerase (PDI) has been characterized by 1H, 13C, and 15N 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 beta-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.

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Year:  1995        PMID： 8580850      PMCID： PMC2143042          DOI： 10.1002/pro.5560041216

Source DB:  PubMed          Journal:  Protein Sci        ISSN： 0961-8368            Impact factor:   6.725


  29 in total

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7.  Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase.

Authors:  N J Darby; T E Creighton
Journal:  Biochemistry       Date:  1995-09-19       Impact factor: 3.162

8.  The interaction of human estrogen receptor with DNA is modulated by receptor-associated proteins.

Authors:  C C Landel; P J Kushner; G L Greene
Journal:  Mol Endocrinol       Date:  1994-10

9.  Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N- and C-terminal domains.

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Journal:  J Biol Chem       Date:  1994-12-09       Impact factor: 5.157

10.  Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene.

Authors:  T Pihlajaniemi; T Helaakoski; K Tasanen; R Myllylä; M L Huhtala; J Koivu; K I Kivirikko
Journal:  EMBO J       Date:  1987-03       Impact factor: 11.598
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  10 in total

1.  Tools for the automated assignment of high-resolution three-dimensional protein NMR spectra based on pattern recognition techniques.

Authors:  D Croft; J Kemmink; K P Neidig; H Oschkinat
Journal:  J Biomol NMR       Date:  1997-10       Impact factor: 2.835

Review 2.  Protein folding in the bacterial periplasm.

Authors:  D Missiakas; S Raina
Journal:  J Bacteriol       Date:  1997-04       Impact factor: 3.490

3.  Small molecule-induced oxidation of protein disulfide isomerase is neuroprotective.

Authors:  Anna Kaplan; Michael M Gaschler; Denise E Dunn; Ryan Colligan; Lewis M Brown; Arthur G Palmer; Donald C Lo; Brent R Stockwell
Journal:  Proc Natl Acad Sci U S A       Date:  2015-04-06       Impact factor: 11.205

4.  The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins.

Authors:  P Klappa; L W Ruddock; N J Darby; R B Freedman
Journal:  EMBO J       Date:  1998-02-16       Impact factor: 11.598

5.  The structure in solution of the b domain of protein disulfide isomerase.

Authors:  J Kemmink; K Dijkstra; M Mariani; R M Scheek; E Penka; M Nilges; N J Darby
Journal:  J Biomol NMR       Date:  1999-04       Impact factor: 2.835

6.  Crystallization and preliminary crystallographic analysis of the complex between triiodothyronine and the bb' fragment of rat protein disulfide isomerase.

Authors:  Shoko Hashimoto; Len Ito; Masaki Okumura; Tomohisa Shibano; Marina Nawata; Takashi Kumasaka; Hiroshi Yamaguchi; Susumu Imaoka
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2012-03-28

7.  Specificity in substrate binding by protein folding catalysts: tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp.

Authors:  L W Ruddock; R B Freedman; P Klappa
Journal:  Protein Sci       Date:  2000-04       Impact factor: 6.725

8.  Differences between the electronic environments of reduced and oxidized Escherichia coli DsbA inferred from heteronuclear magnetic resonance spectroscopy.

Authors:  J Couprie; M L Remerowski; A Bailleul; M Courçon; N Gilles; E Quéméneur; N Jamin
Journal:  Protein Sci       Date:  1998-10       Impact factor: 6.725

9.  The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide.

Authors:  P Koivunen; A Pirneskoski; P Karvonen; J Ljung; T Helaakoski; H Notbohm; K I Kivirikko
Journal:  EMBO J       Date:  1999-01-04       Impact factor: 11.598

10.  Measuring protein reduction potentials using 15N HSQC NMR spectroscopy.

Authors:  Samantha L Taylor; Harriet Crawley-Snowdon; Jane L Wagstaff; Michelle L Rowe; Mark Shepherd; Richard A Williamson; Mark J Howard
Journal:  Chem Commun (Camb)       Date:  2013-01-29       Impact factor: 6.222
  10 in total

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