Homology modelling studies on human galactose-1-phosphate uridylyltransferase and on its galactosemia-related mutant Q188R provide an explanation of molecular effects of the mutation on homo- and heterodimers. (Articolo in rivista)

Type

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

Label

• Homology modelling studies on human galactose-1-phosphate uridylyltransferase and on its galactosemia-related mutant Q188R provide an explanation of molecular effects of the mutation on homo- and heterodimers. (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

Alternative label

• Marabotti A., Facchiano A.M. (2005)
  Homology modelling studies on human galactose-1-phosphate uridylyltransferase and on its galactosemia-related mutant Q188R provide an explanation of molecular effects of the mutation on homo- and heterodimers.
  in Journal of medicinal chemistry
  (literal)

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

• Marabotti A., Facchiano A.M. (literal)

Pagina inizio

• 773 (literal)

Pagina fine

• 779 (literal)

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

• 2 (literal)

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

• 48 (literal)

Rivista

• Journal of medicinal chemistry (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• Homology modelling studies on human galactose-1-phosphate uridylyltransferase and on its galactosemia-related mutant Q188R provide an explanation of molecular effects of the mutation on homo- and heterodimers. (literal)

Abstract

• We have created theoretical models of the three-dimensional dimeric structure of human galactose-1-phosphate uridylyltransferase as well as of homo- and heterodimers carrying the Q188R mutation by using comparative modeling procedures. These mutants are associated to the most frequent form of the genetic disease galactosemia. We have analyzed the impact of this mutation both on enzyme-substrate interactions as well as on interchain interactions in the heterodimers and in the homodimer. We suggest a molecular explanation for the altered function, caused by different enzyme-substrate interactions, and for the partial dominant negative effect of the mutant allele that is present in heterozygotes for this gene, related to a substantial loss of interchain hydrogen bonds. These results can be considered a starting point for a more extensive characterization at the molecular level of the other mutations linked to this genetic disease. (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

• ANNA MARABOTTI (Unità di personale interno)
• ANNA MARABOTTI (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)
• ANNA MARABOTTI (Unità di personale interno)
• ANNA MARABOTTI (Unità di personale esterno)

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

• Journal of medicinal chemistry (Rivista)