Modelling the 3D structure of WSCI. Probing the reactive site of the inhibitor with two susceptible proteinases, by time-course analysis and molecular dynamics simulations. (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Modelling the 3D structure of WSCI. Probing the reactive site of the inhibitor with two susceptible proteinases, by time-course analysis and molecular dynamics simulations. (Articolo in rivista) (literal)

Anno

• 2006-01-01T00:00:00+01:00 (literal)

Alternative label

• Facchiano A, Costantini S, Di Maro A, Panichi D, Chambery A, Parente A, Di Gennaro S, Poerio E (2006)
  Modelling the 3D structure of WSCI. Probing the reactive site of the inhibitor with two susceptible proteinases, by time-course analysis and molecular dynamics simulations.
  in Biological chemistry (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Facchiano A, Costantini S, Di Maro A, Panichi D, Chambery A, Parente A, Di Gennaro S, Poerio E (literal)

Pagina inizio

• 931 (literal)

Pagina fine

• 940 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni

• 1 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 387 (literal)

Rivista

• Biological chemistry (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• Modelling the 3D structure of WSCI. Probing the reactive site of the inhibitor with two susceptible proteinases, by time-course analysis and molecular dynamics simulations. (literal)

Abstract

• Comparative modeling and time-course hydrolysis experiments have been applied to investigate two enzyme-inhibitor complexes formed between the wheat subtilisin-chymotrypsin inhibitor (WSCI) and two susceptible proteinases. WSCI represents the first case of a wheat protein inhibitor active against animal chymotrypsins and bacterial subtilisins. The model was created using as template structure that of the CI-2A inhibitor from barley (PDB code: 2CI2), which shares 87% sequence identity with WSCI. Under these conditions of high similarity, the comparative modeling approach can be successfully applied. We predicted the WSCI 3D model and used it to investigate enzyme-inhibitor complex systems. Experimental observations indicated that chymotrypsin, but not subtilisin, in addition to cleavage at the primary reactive site Met48-Glu49, is able to hydrolyze a second peptide bond between Phe58 and Val59. Here, we report on cleavage of the peptide bond at the inhibitor's reactive site (Met48-Glu49) determined using time-course hydrolysis experiments; the same event was investigated for both subtilisin/WSCI and chymotrypsin/WSCI complexes using molecular dynamics simulations. The molecular details of the initial inhibitor-enzyme interactions, as well as of the changes observed during the simulations, allow us to speculate on the different fates of the two WSCI-proteinase complexes. (literal)

Prodotto di

• Institute of food sciences (ISA) (Istituto)
• Metodologie di Spettrometria di Massa, Proteomica, Metabolomica e Bioinformatica nelle Scienze dell'Alimentazione (AG.P05.003.001) (Modulo)

Autore CNR

• SUSAN COSTANTINI (Unità di personale esterno)
• ANGELO FACCHIANO (Unità di personale interno)

Incoming links:

Prodotto

• Institute of food sciences (ISA) (Istituto)
• Metodologie di Spettrometria di Massa, Proteomica, Metabolomica e Bioinformatica nelle Scienze dell'Alimentazione (AG.P05.003.001) (Modulo)

Autore CNR di

• ANGELO FACCHIANO (Unità di personale interno)
• SUSAN COSTANTINI (Unità di personale esterno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Biological chemistry (Rivista)