WFRF:(Lillig CH)
Search: WFRF:(Lillig CH) > (2020-2021) > Molecular Basis for...
- 1 of 1
- Previous record
- Next record
- To hitlist
Molecular Basis for the Interactions of Human Thioredoxins with Their Respective Reductases
- Hossain, MF (author)
- Bodnar, Y (author)
- Klein, C (author)
- show more...
- Salas, CO (author)
- Gellert, M (author)
- Lillig, CH (author)
- show less...
- (creator_code:org_t)
- Hindawi Limited, 2021
- 2021
- English.
- In: Oxidative medicine and cellular longevity. - : Hindawi Limited. - 1942-0994 .- 1942-0900. ; 2021, s. 6621292-
- Journal article (peer-reviewed)
Abstract
Subject headings
Close
- The mammalian cytosolic thioredoxin (Trx) system consists of Trx1 and its reductase, the NADPH-dependent seleno-enzyme TrxR1. These proteins function as electron donor for metabolic enzymes, for instance in DNA synthesis, and the redox regulation of numerous processes. In this work, we analysed the interactions between these two proteins. We proposed electrostatic complementarity as major force controlling the formation of encounter complexes between the proteins and thus the efficiency of the subsequent electron transfer reaction. If our hypothesis is valid, formation of the encounter complex should be independent of the redox reaction. In fact, we were able to confirm that also a redox inactive mutant of Trx1 lacking both active site cysteinyl residues (C32,35S) binds to TrxR1 in a similar manner and with similar kinetics as the wild-type protein. We have generated a number of mutants with alterations in electrostatic properties and characterised their interaction with TrxR1 in kinetic assays. For human Trx1 and TrxR1, complementary electrostatic surfaces within the area covered in the encounter complex appear to control the affinity of the reductase for its substrate Trx. Electrostatic compatibility was even observed in areas that do not form direct molecular interactions in the encounter complex, and our results suggest that the electrostatic complementarity in these areas influences the catalytic efficiency of the reduction. The human genome encodes ten cytosolic Trx-like or Trx domain-containing proteins. In agreement with our hypothesis, the proteins that have been characterised as TrxR1 substrates also show the highest similarity in their electrostatic properties.
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
- Oxidative medicine and cellular longevity (Search for host publication in LIBRIS)
To the university's database
- 1 of 1
- Previous record
- Next record
- To hitlist
Find more in SwePub
- By the author/editor
- Hossain, MF
- Bodnar, Y
- Klein, C
- Salas, CO
- Arner, ESJ
- Gellert, M
- show more...
- Lillig, CH
- show less...
- Articles in the publication
- Oxidative medici ...
- By the university
- Karolinska Institutet
Search outside SwePub
- Extend your search to:
- Google Book Search
- Google Scholar
Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.
- Copyright © LIBRIS - National Library Systems
- LIBRIS.kb.se
