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Digital archive of theses discussed at the University of Pisa

 

Thesis etd-01162006-134718


Thesis type
Tesi di dottorato di ricerca
Author
Alpi, Emanuele
URN
etd-01162006-134718
Thesis title
Deciphering PDZ mediated protein complexes by Affinity Chromatography and Mass Spectrometry
Academic discipline
CHIM/06
Course of study
SCIENZE CHIMICHE
Supervisors
relatore Prof. Salvadori, Piero
relatore Prof. Dente, Luciana
Keywords
  • affinity chromatography
  • MALDI peptide mapping
  • MS
  • PATJ
  • PDZ domains
Graduation session start date
07/03/2006
Availability
Withheld
Release date
07/03/2046
Summary
Small modular binding domains mediate protein-protein interactions by conferring specificity in multiprotein complex formation. The variability of PDZ (PSD-95/Dlg/ZO-1) domains primary sequences and the structural adaptability of their fold results in different binding modalities. PDZs generally bind to the target carboxyl terminus, but they can also bind to internal sequences of other PDZ or other interaction modules. The eight PDZ domains of the protein PATJ (Protein Associated to Tight Junctions) have been assayed with protein extracts by affinity chromatography followed by mass spectrometry in order to find their protein interactors. Fifteen different proteins were indentified and the interactions of some of them with the PDZ domains of PATJ were further investigated
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