http://www.cnr.it/ontology/cnr/individuo/prodotto/ID14195
Multiple catalytically active thioredoxin folds: a winning strategy for many functions. (Articolo in rivista)
- Type
- Label
- Multiple catalytically active thioredoxin folds: a winning strategy for many functions. (Articolo in rivista) (literal)
- Anno
- 2010-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1007/s00018-010-0449-9 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Pedone E; Limauro D; D'Ambrosio K; De Simone G; Bartolucci S (literal)
- Pagina inizio
- Pagina fine
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
- Rivista
- Note
- Scopu (literal)
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Naples, Italy
Dipartimento di Biologia Strutturale e Funzionale, Università degli Studi di Napoli ''Federico II'', Complesso Universitario Monte S. Angelo, Via Cinthia, 80126 Naples, Italy (literal)
- Titolo
- Multiple catalytically active thioredoxin folds: a winning strategy for many functions. (literal)
- Abstract
- The Thioredoxin (Trx) fold is a versatile protein scaffold consisting of a four-stranded b-sheet surrounded by three a-helices. Various insertions are possible on this
structural theme originating different proteins, which show a variety of functions and specificities. During evolution, the assembly of different Trx fold domains has been used many times to build new multi-domain proteins able to perform a large number of catalytic functions. To clarify the interaction mode of the different Trx domains within a multi-domain structure and how their combination can affect catalytic performances, in this review, we report on a structural and functional analysis of the most representative proteins containing more than one catalytically active Trx domain: the eukaryotic protein disulfide isomerases (PDIs), the thermophilic protein disulfide oxidoreductases (PDOs) and the hybrid peroxiredoxins (Prxs). (literal)
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- Autore CNR
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