• norsk
    • English
  • norsk 
    • norsk
    • English
  • Logg inn
Vis innførsel 
  •   Hjem
  • Øvrige samlinger
  • Publikasjoner fra CRIStin - NTNU
  • Vis innførsel
  •   Hjem
  • Øvrige samlinger
  • Publikasjoner fra CRIStin - NTNU
  • Vis innførsel
JavaScript is disabled for your browser. Some features of this site may not work without it.

Structural Analysis of Glutaredoxin Domain of Mus musculus Thioredoxin Glutathione Reductase

Dobrovolska, Olena; Shumilina, Elena; Gladyshev, Vadim N.; Dikiy, Alexander
Journal article, Peer reviewed
Thumbnail
Åpne
fetchObject8402.pdf (730.3Kb)
Permanent lenke
http://hdl.handle.net/11250/2365569
Utgivelsesdato
2012
Metadata
Vis full innførsel
Samlinger
  • Institutt for bioteknologi og matvitenskap [900]
  • Publikasjoner fra CRIStin - NTNU [20955]
Originalversjon
PLoS ONE 2012, 7(12)   10.1371/journal.pone.0052914
Sammendrag
Thioredoxin glutathione reductase (TGR) is a member of the mammalian thioredoxin reductase family that has a monothiol

glutaredoxin (Grx) domain attached to the thioredoxin reductase module. Here, we report a structure of the Grx domain of

mouse TGR, determined through high resolution NMR spectroscopy to the final backbone RMSD value of 0.4860.10 A°

. The

structure represents a sandwich-like molecule composed of a four stranded b-sheet flanked by five a–helixes, with the CxxS

active motif located on the catalytic loop. We structurally characterized the glutathione-binding site in the protein and

describe sequence and structural relationships of the domain with glutaredoxins. The structure illuminates a key functional

center that evolved in mammalian TGRs to act in thiol-disulfide reactions. Our study allows us to hypothesize that Cys105

might be functionally relevant for TGR catalysis. In addition, the data suggest that the N-terminus of Grx acts as a possible

regulatory signal also protecting the protein active site from unwanted interactions in cellular cytosol.
Utgiver
Public Library of Science
Tidsskrift
PLoS ONE

Kontakt oss | Gi tilbakemelding

Personvernerklæring
DSpace software copyright © 2002-2019  DuraSpace

Levert av  Unit
 

 

Bla i

Hele arkivetDelarkiv og samlingerUtgivelsesdatoForfattereTitlerEmneordDokumenttyperTidsskrifterDenne samlingenUtgivelsesdatoForfattereTitlerEmneordDokumenttyperTidsskrifter

Min side

Logg inn

Statistikk

Besøksstatistikk

Kontakt oss | Gi tilbakemelding

Personvernerklæring
DSpace software copyright © 2002-2019  DuraSpace

Levert av  Unit