An Unprecedented Catalytic Motif Revealed in the Model Structure of Amide Hydrolyzing Antibody 312d6

Fabio Benedetti, Federico Berti, Kevin Brady, Alfonso Colombatti, Alessandro Pauletto, Carlo Pucillo, Neil R. Thomas

Research output: Contribution to journalArticle

Abstract

An arginine dyad: A homology model of catalytic antibody 312D6 sets the rationale for the antibody's amidase activity. Docking of a sulfonamide hapten to the model highlights the role of an arginine dyad in binding and catalysis. This catalytic motif is unprecedented in antibody catalysis.

Original languageEnglish
Pages (from-to)129-131
Number of pages3
JournalChemBioChem
Volume5
Issue number1
DOIs
Publication statusPublished - Jan 3 2004

Keywords

  • Amides
  • Catalytic antibodies
  • Homology model
  • Hydrolysis
  • Sulfonamides

ASJC Scopus subject areas

  • Drug Discovery
  • Organic Chemistry
  • Biochemistry, Genetics and Molecular Biology(all)

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    Benedetti, F., Berti, F., Brady, K., Colombatti, A., Pauletto, A., Pucillo, C., & Thomas, N. R. (2004). An Unprecedented Catalytic Motif Revealed in the Model Structure of Amide Hydrolyzing Antibody 312d6. ChemBioChem, 5(1), 129-131. https://doi.org/10.1002/cbic.200300738