Prolyl oligopeptidase: An unusual β-propeller domain regulates proteolysis

Vilmos Fülöp, Zsolt Böcskei, László Polgár

Research output: Contribution to journalArticle

421 Citations (Scopus)


Prolyl oligopeptidase is a large cytosolic enzyme that belongs to a new class of serine peptidases. The enzyme is involved in the maturation and degradation of peptide hormones and neuropeptides, which relate to the induction of amnesia. The 1.4 Å resolution crystal structure is presented here. The enzyme contains a peptidase domain with an α/β hydrolase fold, and its catalytic triad (Ser554, His680, Asp641) is covered by the central tunnel of an unusual β propeller. This domain makes prolyl oligopeptidase an oligopeptidase by excluding large structured peptides from the active site. In this way, the propeller protects larger peptides and proteins from proteolysis in the cytosol. The structure is also obtained with a transition state inhibitor, which may facilitate drug design to treat memory disorders.

Original languageEnglish
Pages (from-to)161-170
Number of pages10
Issue number2
Publication statusPublished - Jul 24 1998

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Fingerprint Dive into the research topics of 'Prolyl oligopeptidase: An unusual β-propeller domain regulates proteolysis'. Together they form a unique fingerprint.

  • Cite this