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PDBsum entry 1cqg

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protein Protein-protein interface(s) links
Complex (electron transport/peptide) PDB id
1cqg
Jmol
Contents
Protein chains
105 a.a. *
13 a.a. *
* Residue conservation analysis
PDB id:
1cqg
Name: Complex (electron transport/peptide)
Title: 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 ref-1 (residues 59-71 of the p50 subunit of nfkb), nmr, 31 structures
Structure: Thioredoxin. Chain: a. Engineered: yes. Mutation: yes. Ref-1 peptide. Chain: b. Fragment: residues 59 - 71 of the p50 subunit of nfkb. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: potential.
NMR struc: 35 models
Authors: G.M.Clore,J.Qin,A.M.Gronenborn
Key ref:
J.Qin et al. (1996). The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal. Structure, 4, 613-620. PubMed id: 8736558 DOI: 10.1016/S0969-2126(96)00065-2
Date:
02-Apr-96     Release date:   01-Aug-96    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P10599  (THIO_HUMAN) -  Thioredoxin
Seq:
Struc:
105 a.a.
105 a.a.*
Protein chain
Pfam   ArchSchema ?
P27695  (APEX1_HUMAN) -  DNA-(apurinic or apyrimidinic site) lyase
Seq:
Struc:
318 a.a.
13 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain B: E.C.4.2.99.18  - DNA-(apurinic or apyrimidinic site) lyase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   7 terms 
  Biological process     nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway   19 terms 
  Biochemical function     protein binding     4 terms  

 

 
DOI no: 10.1016/S0969-2126(96)00065-2 Structure 4:613-620 (1996)
PubMed id: 8736558  
 
 
The solution structure of human thioredoxin complexed with its target from Ref-1 reveals peptide chain reversal.
J.Qin, G.M.Clore, W.P.Kennedy, J.Kuszewski, A.M.Gronenborn.
 
  ABSTRACT  
 
BACKGROUND: Human thioredoxin (hTRX) is a 12 kDa cellular redox protein that has been shown to play an important role in the activation of a number of transcriptional and translational regulators via a thiol-redox mechanism. This activity may be direct or indirect via another redox protein known as Ref-1. The structure of a complex of hTRX with a peptide comprising its target from the transcription factor NF kappa B has previously been solved. To further extend our knowledge of the recognition by and interaction of hTRX with its various targets, we have studied a complex between hTRX and a Ref-1 peptide. This complex represents a kinetically stable mixed disulfide intermediate along the reaction pathway. RESULTS: Using multidimensional heteronuclear edited and filtered NMR spectroscopy, we have solved the solution structure of a complex between hTRX and a 13-residue peptide comprising residues 59-71 of Ref-1. The Ref-1 peptide is located in a crescent-shaped groove on the surface of hTRX, the groove being formed by residues in the active-site loop (residues 32-36), helix 3, beta strands 3 and 5, and the loop between beta strands 3 and 4. The complex is stabilized by numerous hydrogen-bonding and hydrophobic interactions that involve residues 61-69 of the peptide and confer substrate specificity. CONCLUSIONS: The orientation of the Ref-1 peptide in the hTRX-Ref-1 complex is opposite to that found in the previously solved complex of hTRX with the target peptide from the transcription factor NF kappa B. Orientation is determined by three discriminating interactions involving the nature of the residues at the P-2' P-4 and P-5 binding positions. (P0 defines the active cysteine of the peptide, Cys65 for Ref-1 and Cys62 for NF kappa B. Positive and negative numbers indicate residues N-terminal and C-terminal to this residue, respectively, and vice versa for NF kappa B as it binds in the opposite orientation.) The environment surrounding the reactive Cys32 of hTRX, as well as the packing of the P+3 to P-4 residues are essentially the same in the two complexes, despite the opposing orientation of the peptide chains. This versatility in substrate recognition permits hTRX to act as a wide-ranging redox regulator for the cell.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. Stereoview showing the interactions between the Ref-1 peptide and hTRX. The backbones (N, Cα, C) of hTRX and the Ref-1 peptide are shown in blue and red, respectively; the side chains of hTRX and the Ref-1 peptide at the interface of the complex are shown in magenta and green, respectively; and the disulfide bond between Cys32 of hTRX and cys62 of the Ref-1 peptide is shown in yellow. Figure 3. Stereoview showing the interactions between the Ref-1 peptide and hTRX. The backbones (N, Cα, C) of hTRX and the Ref-1 peptide are shown in blue and red, respectively; the side chains of hTRX and the Ref-1 peptide at the interface of the complex are shown in magenta and green, respectively; and the disulfide bond between Cys32 of hTRX and cys62 of the Ref-1 peptide is shown in yellow. (The figure was generated with the program VISP [3][44].)
Figure 5.
Figure 5. Schematic summary of the interactions observed in the hTRX–Ref-1 and hTRX–NFκB complexes. (a) All interactions with the exception of those involving backbone–backbone hydrogen bonds: hydrophobic, hydrogen-bonding and salt bridge interactions are represented by continuous (—), long dashed (– – –) and short dashed (- - -) lines, respectively. (b) Backbone–backbone hydrogen bonds. Figure 5. Schematic summary of the interactions observed in the hTRX–Ref-1 and hTRX–NFκB complexes. (a) All interactions with the exception of those involving backbone–backbone hydrogen bonds: hydrophobic, hydrogen-bonding and salt bridge interactions are represented by continuous (—), long dashed (– – –) and short dashed (- - -) lines, respectively. (b) Backbone–backbone hydrogen bonds.
 
  The above figures are reprinted by permission from Cell Press: Structure (1996, 4, 613-620) copyright 1996.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20981751 G.Hall, T.D.Bradshaw, C.A.Laughton, M.F.Stevens, and J.Emsley (2011).
Structure of Mycobacterium tuberculosis thioredoxin in complex with quinol inhibitor PMX464.
  Protein Sci, 20, 210-215.
PDB codes: 3nof 3o6t
20662007 A.Weichsel, M.Kem, and W.R.Montfort (2010).
Crystal structure of human thioredoxin revealing an unraveled helix and exposed S-nitrosation site.
  Protein Sci, 19, 1801-1806.
PDB codes: 3m9j 3m9k
20625793 E.Pedone, D.Limauro, K.D'Ambrosio, G.De Simone, and S.Bartolucci (2010).
Multiple catalytically active thioredoxin folds: a winning strategy for many functions.
  Cell Mol Life Sci, 67, 3797-3814.  
19535335 A.Crow, A.Lewin, O.Hecht, M.Carlsson Möller, G.R.Moore, L.Hederstedt, and N.E.Le Brun (2009).
Crystal structure and biophysical properties of Bacillus subtilis BdbD. An oxidizing thiol:disulfide oxidoreductase containing a novel metal site.
  J Biol Chem, 284, 23719-23733.
PDB codes: 3eu3 3eu4 3gh9 3gha
19692331 C.Wakita, T.Maeshima, A.Yamazaki, T.Shibata, S.Ito, M.Akagawa, M.Ojika, J.Yodoi, and K.Uchida (2009).
Stereochemical configuration of 4-hydroxy-2-nonenal-cysteine adducts and their stereoselective formation in a redox-regulated protein.
  J Biol Chem, 284, 28810-28822.  
19675666 G.Roos, N.Foloppe, K.Van Laer, L.Wyns, L.Nilsson, P.Geerlings, and J.Messens (2009).
How thioredoxin dissociates its mixed disulfide.
  PLoS Comput Biol, 5, e1000461.  
18976116 G.Tell, F.Quadrifoglio, C.Tiribelli, and M.R.Kelley (2009).
The many functions of APE1/Ref-1: not only a DNA repair enzyme.
  Antioxid Redox Signal, 11, 601-620.  
19389711 J.J.Paxman, N.A.Borg, J.Horne, P.E.Thompson, Y.Chin, P.Sharma, J.S.Simpson, J.Wielens, S.Piek, C.M.Kahler, H.Sakellaris, M.Pearce, S.P.Bottomley, J.Rossjohn, and M.J.Scanlon (2009).
The structure of the bacterial oxidoreductase enzyme DsbA in complex with a peptide reveals a basis for substrate specificity in the catalytic cycle of DsbA enzymes.
  J Biol Chem, 284, 17835-17845.
PDB code: 3dks
19572737 J.Liang, and J.M.Fernández (2009).
Mechanochemistry: One Bond at a Time.
  ACS Nano, 3, 1628-1645.  
18715144 K.K.Bhakat, A.K.Mantha, and S.Mitra (2009).
Transcriptional regulatory functions of mammalian AP-endonuclease (APE1/Ref-1), an essential multifunctional protein.
  Antioxid Redox Signal, 11, 621-638.  
19182799 L.Banci, I.Bertini, C.Cefaro, S.Ciofi-Baffoni, A.Gallo, M.Martinelli, D.P.Sideris, N.Katrakili, and K.Tokatlidis (2009).
MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria.
  Nat Struct Mol Biol, 16, 198-206.
PDB code: 2k3j
19597482 R.Perez-Jimenez, J.Li, P.Kosuri, I.Sanchez-Romero, A.P.Wiita, D.Rodriguez-Larrea, A.Chueca, A.Holmgren, A.Miranda-Vizuete, K.Becker, S.H.Cho, J.Beckwith, E.Gelhaye, J.P.Jacquot, E.Gaucher, J.M.Sanchez-Ruiz, B.J.Berne, and J.M.Fernandez (2009).
Diversity of chemical mechanisms in thioredoxin catalysis revealed by single-molecule force spectroscopy.
  Nat Struct Mol Biol, 16, 890-896.  
19237745 Y.Carius, D.Rother, C.G.Friedrich, and A.J.Scheidig (2009).
The structure of the periplasmic thiol-disulfide oxidoreductase SoxS from Paracoccus pantotrophus indicates a triple Trx/Grx/DsbC functionality in chemotrophic sulfur oxidation.
  Acta Crystallogr D Biol Crystallogr, 65, 229-240.  
18077463 B.Heras, M.Kurz, R.Jarrott, S.R.Shouldice, P.Frei, G.Robin, M.Cemazar, L.Thöny-Meyer, R.Glockshuber, and J.L.Martin (2008).
Staphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative folding.
  J Biol Chem, 283, 4261-4271.
PDB codes: 3bci 3bck 3bd2
18302150 G.Hernández, J.S.Anderson, and D.M.LeMaster (2008).
Electrostatic stabilization and general base catalysis in the active site of the human protein disulfide isomerase a domain monitored by hydrogen exchange.
  Chembiochem, 9, 768-778.  
18586825 K.Ando, S.Hirao, Y.Kabe, Y.Ogura, I.Sato, Y.Yamaguchi, T.Wada, and H.Handa (2008).
A new APE1/Ref-1-dependent pathway leading to reduction of NF-kappaB and AP-1, and activation of their DNA-binding activity.
  Nucleic Acids Res, 36, 4327-4336.  
18424513 K.Maeda, P.Hägglund, C.Finnie, B.Svensson, and A.Henriksen (2008).
Crystal structures of barley thioredoxin h isoforms HvTrxh1 and HvTrxh2 reveal features involved in protein recognition and possibly in discriminating the isoform specificity.
  Protein Sci, 17, 1015-1024.
PDB codes: 2vlt 2vlu 2vlv 2vm1 2vm2
18703840 L.M.Gibson, N.N.Dingra, C.E.Outten, and L.Lebioda (2008).
Structure of the thioredoxin-like domain of yeast glutaredoxin 3.
  Acta Crystallogr D Biol Crystallogr, 64, 927-932.
PDB code: 3d6i
18757366 T.H.Elgán, and K.D.Berndt (2008).
Quantifying Escherichia coli Glutaredoxin-3 Substrate Specificity Using Ligand-induced Stability.
  J Biol Chem, 283, 32839-32847.  
18455736 T.R.Kouwen, J.Andréll, R.Schrijver, J.Y.Dubois, M.J.Maher, S.Iwata, E.P.Carpenter, and J.M.van Dijl (2008).
Thioredoxin A active-site mutants form mixed disulfide dimers that resemble enzyme-substrate reaction intermediates.
  J Mol Biol, 379, 520-534.
PDB code: 2voc
18003611 T.T.Mac, A.von Hacht, K.C.Hung, R.J.Dutton, D.Boyd, J.C.Bardwell, and T.S.Ulmer (2008).
Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase.
  J Biol Chem, 283, 824-832.
PDB code: 2ju5
17972886 A.P.Wiita, R.Perez-Jimenez, K.A.Walther, F.Gräter, B.J.Berne, A.Holmgren, J.M.Sanchez-Ruiz, and J.M.Fernandez (2007).
Probing the chemistry of thioredoxin catalysis with force.
  Nature, 450, 124-127.  
17303556 Y.Li, Y.Hu, X.Zhang, H.Xu, E.Lescop, B.Xia, and C.Jin (2007).
Conformational fluctuations coupled to the thiol-disulfide transfer between thioredoxin and arsenate reductase in Bacillus subtilis.
  J Biol Chem, 282, 11078-11083.
PDB codes: 2gzy 2gzz 2ipa
16971393 A.Lewin, A.Crow, A.Oubrie, and N.E.Le Brun (2006).
Molecular basis for specificity of the extracytoplasmic thioredoxin ResA.
  J Biol Chem, 281, 35467-35477.
PDB codes: 2h19 2h1a 2h1b 2h1d 2h1g
17139080 G.Hall, M.Shah, P.A.McEwan, C.Laughton, M.Stevens, A.Westwell, and J.Emsley (2006).
Structure of Mycobacterium tuberculosis thioredoxin C.
  Acta Crystallogr D Biol Crystallogr, 62, 1453-1457.
PDB code: 2i1u
16840349 H.P.Su, D.Y.Lin, and D.N.Garboczi (2006).
The structure of G4, the poxvirus disulfide oxidoreductase essential for virus maturation and infectivity.
  J Virol, 80, 7706-7713.
PDB code: 2g2q
17034356 J.Yoshioka, E.R.Schreiter, and R.T.Lee (2006).
Role of thioredoxin in cell growth through interactions with signaling molecules.
  Antioxid Redox Signal, 8, 2143-2151.  
16766796 P.Patwari, L.J.Higgins, W.A.Chutkow, J.Yoshioka, and R.T.Lee (2006).
The interaction of thioredoxin with Txnip. Evidence for formation of a mixed disulfide by disulfide exchange.
  J Biol Chem, 281, 21884-21891.  
16930136 R.Ladenstein, and B.Ren (2006).
Protein disulfides and protein disulfide oxidoreductases in hyperthermophiles.
  FEBS J, 273, 4170-4185.  
16677078 S.Mkrtchian, and T.Sandalova (2006).
ERp29, an unusual redox-inactive member of the thioredoxin family.
  Antioxid Redox Signal, 8, 325-337.  
17007870 T.Ago, and J.Sadoshima (2006).
Thioredoxin and ventricular remodeling.
  J Mol Cell Cardiol, 41, 762-773.  
16418167 X.Zhang, Y.Hu, X.Guo, E.Lescop, Y.Li, B.Xia, and C.Jin (2006).
The Bacillus subtilis YkuV is a thiol:disulfide oxidoreductase revealed by its redox structures and activity.
  J Biol Chem, 281, 8296-8304.
PDB codes: 2b5x 2b5y
15946192 A.Catania, P.Grieco, A.Randazzo, E.Novellino, S.Gatti, C.Rossi, G.Colombo, and J.M.Lipton (2005).
Three-dimensional structure of the alpha-MSH-derived candidacidal peptide [Ac-CKPV]2.
  J Pept Res, 66, 19-26.  
15706084 G.Tell, G.Damante, D.Caldwell, and M.R.Kelley (2005).
The intracellular localization of APE1/Ref-1: more than a passive phenomenon?
  Antioxid Redox Signal, 7, 367-384.  
15687218 H.Kadokura, L.Nichols, and J.Beckwith (2005).
Mutational alterations of the key cis proline residue that cause accumulation of enzymatic reaction intermediates of DsbA, a member of the thioredoxin superfamily.
  J Bacteriol, 187, 1519-1522.  
14739460 H.Kadokura, H.Tian, T.Zander, J.C.Bardwell, and J.Beckwith (2004).
Snapshots of DsbA in action: detection of proteins in the process of oxidative folding.
  Science, 303, 534-537.  
15355959 J.R.Woo, S.J.Kim, W.Jeong, Y.H.Cho, S.C.Lee, Y.J.Chung, S.G.Rhee, and S.E.Ryu (2004).
Structural basis of cellular redox regulation by human TRP14.
  J Biol Chem, 279, 48120-48125.
PDB code: 1wou
12529327 S.J.Kim, J.R.Woo, Y.S.Hwang, D.G.Jeong, D.H.Shin, K.Kim, and S.E.Ryu (2003).
The tetrameric structure of Haemophilus influenza hybrid Prx5 reveals interactions between electron donor and acceptor proteins.
  J Biol Chem, 278, 10790-10798.
PDB code: 1nm3
12816947 W.H.Watson, J.Pohl, W.R.Montfort, O.Stuchlik, M.S.Reed, G.Powis, and D.P.Jones (2003).
Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif.
  J Biol Chem, 278, 33408-33415.  
11809897 D.T.Kuninger, T.Izumi, J.Papaconstantinou, and S.Mitra (2002).
Human AP-endonuclease 1 and hnRNP-L interact with a nCaRE-like repressor element in the AP-endonuclease 1 promoter.
  Nucleic Acids Res, 30, 823-829.  
12401497 E.Lazoura, W.Campbell, Y.Yamaguchi, K.Kato, N.Okada, and H.Okada (2002).
Rational structure-based design of a novel carboxypeptidase R inhibitor.
  Chem Biol, 9, 1129-1139.  
11985582 J.Jin, X.Chen, Y.Zhou, M.Bartlam, Q.Guo, Y.Liu, Y.Sun, Y.Gao, S.Ye, G.Li, Z.Rao, B.Qiang, and J.Yuan (2002).
Crystal structure of the catalytic domain of a human thioredoxin-like protein.
  Eur J Biochem, 269, 2060-2068.
PDB code: 1gh2
12230868 K.Ejima, M.D.Layne, I.M.Carvajal, H.Nanri, B.Ith, S.F.Yet, and M.A.Perrella (2002).
Modulation of the thioredoxin system during inflammatory responses and its effect on heme oxygenase-1 expression.
  Antioxid Redox Signal, 4, 569-575.  
  12074972 K.Hirota, H.Nakamura, H.Masutani, and J.Yodoi (2002).
Thioredoxin superfamily and thioredoxin-inducing agents.
  Ann N Y Acad Sci, 957, 189-199.  
  12076971 L.E.Shao, T.Tanaka, R.Gribi, and J.Yu (2002).
Thioredoxin-related regulation of NO/NOS activities.
  Ann N Y Acad Sci, 962, 140-150.  
11980496 T.L.Nguyen, and E.Breslow (2002).
NMR analysis of the monomeric form of a mutant unliganded bovine neurophysin: comparison with the crystal structure of a neurophysin dimer.
  Biochemistry, 41, 5920-5930.
PDB codes: 1l5c 1l5d
11347894 B.Hofmann, H.Budde, K.Bruns, S.A.Guerrero, H.M.Kalisz, U.Menge, M.Montemartini, E.Nogoceke, P.Steinert, J.B.Wissing, L.Flohé, and H.J.Hecht (2001).
Structures of tryparedoxins revealing interaction with trypanothione.
  Biol Chem, 382, 459-471.
PDB codes: 1ewx 1ezk 1fg4 1i5g
11264458 G.Powis, and W.R.Montfort (2001).
Properties and biological activities of thioredoxins.
  Annu Rev Pharmacol Toxicol, 41, 261-295.  
11441809 G.Powis, and W.R.Montfort (2001).
Properties and biological activities of thioredoxins.
  Annu Rev Biophys Biomol Struct, 30, 421-455.  
10671489 D.Lando, I.Pongratz, L.Poellinger, and M.L.Whitelaw (2000).
A redox mechanism controls differential DNA binding activities of hypoxia-inducible factor (HIF) 1alpha and the HIF-like factor.
  J Biol Chem, 275, 4618-4627.  
10828992 J.Couprie, F.Vinci, C.Dugave, E.Quéméneur, and M.Moutiez (2000).
Investigation of the DsbA mechanism through the synthesis and analysis of an irreversible enzyme-ligand complex.
  Biochemistry, 39, 6732-6742.  
10998255 J.M.Richardson, S.D.Lemaire, J.P.Jacquot, and G.I.Makhatadze (2000).
Difference in the mechanisms of the cold and heat induced unfolding of thioredoxin h from Chlamydomonas reinhardtii: spectroscopic and calorimetric studies.
  Biochemistry, 39, 11154-11162.  
11213487 J.Qin, Y.Yang, A.Velyvis, and A.Gronenborn (2000).
Molecular views of redox regulation: three-dimensional structures of redox regulatory proteins and protein complexes.
  Antioxid Redox Signal, 2, 827-840.  
11582571 V.Menchise, C.Corbier, C.Didierjean, J.P.Jacquot, E.Benedetti, M.Saviano, and A.Aubry (2000).
Crystal structure of the W35A mutant thioredoxin h from Chlamydomonas reinhardtii: the substitution of the conserved active site Trp leads to modifications in the environment of the two catalytic cysteines.
  Biopolymers, 56, 1-7.  
10523305 C.Gaiddon, N.C.Moorthy, and C.Prives (1999).
Ref-1 regulates the transactivation and pro-apoptotic functions of p53 in vivo.
  EMBO J, 18, 5609-5621.  
11233142 H.Tanaka, Y.Makino, K.Okamoto, T.Iida, K.Yan, and N.Yoshikawa (1999).
Redox regulation of the glucocorticoid receptor.
  Antioxid Redox Signal, 1, 403-423.  
  10210188 J.B.Charbonnier, P.Belin, M.Moutiez, E.A.Stura, and E.Quéméneur (1999).
On the role of the cis-proline residue in the active site of DsbA.
  Protein Sci, 8, 96.
PDB code: 1bq7
10488136 K.Hirota, M.Murata, Y.Sachi, H.Nakamura, J.Takeuchi, K.Mori, and J.Yodoi (1999).
Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-kappaB.
  J Biol Chem, 274, 27891-27897.  
10194350 K.Johansson, S.Ramaswamy, M.Saarinen, M.Lemaire-Chamley, E.Issakidis-Bourguet, M.Miginiac-Maslow, and H.Eklund (1999).
Structural basis for light activation of a chloroplast enzyme: the structure of sorghum NADP-malate dehydrogenase in its oxidized form.
  Biochemistry, 38, 4319-4326.
PDB code: 7mdh
10464297 M.S.Alphey, G.A.Leonard, D.G.Gourley, E.Tetaud, A.H.Fairlamb, and W.N.Hunter (1999).
The high resolution crystal structure of recombinant Crithidia fasciculata tryparedoxin-I.
  J Biol Chem, 274, 25613-25622.
PDB code: 1qk8
10497208 S.Izawa, K.Maeda, K.Sugiyama, J.Mano, Y.Inoue, and A.Kimura (1999).
Thioredoxin deficiency causes the constitutive activation of Yap1, an AP-1-like transcription factor in Saccharomyces cerevisiae.
  J Biol Chem, 274, 28459-28465.  
9665175 B.Ren, G.Tibbelin, D.de Pascale, M.Rossi, S.Bartolucci, and R.Ladenstein (1998).
A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units.
  Nat Struct Biol, 5, 602-611.
PDB code: 1a8l
9782121 M.Hotta, F.Tashiro, H.Ikegami, H.Niwa, T.Ogihara, J.Yodoi, and J.Miyazaki (1998).
Pancreatic beta cell-specific expression of thioredoxin, an antioxidative and antiapoptotic protein, prevents autoimmune and streptozotocin-induced diabetes.
  J Exp Med, 188, 1445-1451.  
9558318 M.J.Berardi, C.L.Pendred, and J.H.Bushweller (1998).
Preparation, characterization, and complete heteronuclear NMR resonance assignments of the glutaredoxin (C14S)-ribonucleotide reductase B1 737-761 (C754S) mixed disulfide.
  Biochemistry, 37, 5849-5857.  
9501259 N.Mouaheb, D.Thomas, L.Verdoucq, P.Monfort, and Y.Meyer (1998).
In vivo functional discrimination between plant thioredoxins by heterologous expression in the yeast Saccharomyces cerevisiae.
  Proc Natl Acad Sci U S A, 95, 3312-3317.  
9463371 P.Klappa, L.W.Ruddock, N.J.Darby, and R.B.Freedman (1998).
The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins.
  EMBO J, 17, 927-935.  
9422728 W.K.Hansen, W.A.Deutsch, A.Yacoub, Y.Xu, D.A.Williams, and M.R.Kelley (1998).
Creation of a fully functional human chimeric DNA repair protein. Combining O6-methylguanine DNA methyltransferase (MGMT) and AP endonuclease (APE/redox effector factor 1 (Ref 1)) DNA repair proteins.
  J Biol Chem, 273, 756-762.  
  9194175 L.W.Guddat, J.C.Bardwell, T.Zander, and J.L.Martin (1997).
The uncharged surface features surrounding the active site of Escherichia coli DsbA are conserved and are implicated in peptide binding.
  Protein Sci, 6, 1148-1156.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.