UNSPECIFIED. (1998) Prolyl oligopeptidase: An unusual beta-propeller domain regulates proteolysis. CELL, 94 (2). pp. 161-170. ISSN 0092-8674

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Abstract

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 Angstrom resolution crystal structure is presented here. The enzyme contains a peptidase domain with an alpha/beta hydrolase fold, and its catalytic triad (Ser554, His680, Asp641) is covered by. the central tunnel of an unusual beta 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.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology
Journal or Publication Title:	CELL
Publisher:	CELL PRESS
ISSN:	0092-8674
Official Date:	24 July 1998
Dates:	Date Event 24 July 1998 UNSPECIFIED
Volume:	94
Number:	2
Number of Pages:	10
Page Range:	pp. 161-170
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/15532

Data sourced from Thomson Reuters' Web of Knowledge

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