Conformational constraints of tyrosine in protein tyrosine kinase substrates: Information about preferred bioactive side-chain orientation (Articolo in rivista)

Type

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

Label

• Conformational constraints of tyrosine in protein tyrosine kinase substrates: Information about preferred bioactive side-chain orientation (Articolo in rivista) (literal)

Anno

• 2003-01-01T00:00:00+01:00 (literal)

Alternative label

• Ruzza P., Calderan A., Donella-Deana A., Biondi B., Cesaro L., Osler A., Elardo S., Guiotto A., Pinna L.A., Borin G. (2003)
  Conformational constraints of tyrosine in protein tyrosine kinase substrates: Information about preferred bioactive side-chain orientation
  in Biopolymers (Print)
  (literal)

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

• Ruzza P., Calderan A., Donella-Deana A., Biondi B., Cesaro L., Osler A., Elardo S., Guiotto A., Pinna L.A., Borin G. (literal)

Pagina inizio

• 478 (literal)

Pagina fine

• 488 (literal)

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

• 71 (literal)

Rivista

• Biopolymers (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• Conformational constraints of tyrosine in protein tyrosine kinase substrates: Information about preferred bioactive side-chain orientation (literal)

Abstract

• The side-chain orientation of a tyrosine residue located in a peptide, which is an excellent substrate of Syk tyrosine kinase (A. M. Brunati, A. Donella-Deana, M. Ruzzene, O. Marin, L. A. Pinna, FEBS Letters, 1995, Vol. 367, pp. 149-152), was fixed in the gauche (+) or gauche (-) conformation by using the 7-hydroxy-1,2,3,4-tetrahydro isoquinoline-3-carboxylic (Htc) structure. The tyrosine trans conformation was blocked by using an aminobenzazepine-type (Hba) structure. The proposed side-chain orientations were confirmed by the analysis of the 1H-NMR parameters: chemical shifts, coupling constants, and nuclear Overhauser effects to the tyrosine constraints in the different analogs. This rotamer scan of the phosphorylatable residue allowed us to generate optimal substrates in terms of both phosphorylation efficiency and selectivity for Syk tyrosine kinase. In contrast, these conformationally restricted tyrosine analogs were not tolerated by the Src-related tyrosine kinases Lyn and c-Fgr. (literal)

Prodotto di

• Istituto di chimica biomolecolare (ICB) (Istituto)

Autore CNR

• ANDREA GUIOTTO (Unità di personale interno)
• ANDREA CALDERAN (Unità di personale interno)
• BARBARA BIONDI (Unità di personale interno)
• GIANFRANCO BORIN (Persona)
• PAOLO RUZZA (Persona)

Incoming links:

Autore CNR di

• ANDREA GUIOTTO (Unità di personale interno)
• PAOLO RUZZA (Persona)
• ANDREA CALDERAN (Unità di personale interno)
• BARBARA BIONDI (Unità di personale interno)
• GIANFRANCO BORIN (Persona)

Prodotto

• Istituto di chimica biomolecolare (ICB) (Istituto)

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

• Biopolymers (Rivista)