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Prolyl oligopeptidase structure and dynamics
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Rea, Dean and Fülöp, Vilmos (2011) Prolyl oligopeptidase structure and dynamics. CNS & Neurological Disorders - Drug Targets, Vol.10 (No.3). pp. 306-310. ISSN 1871-5273.
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Official URL: http://www.bentham.org/cdtcnsnd
Abstract
Prolyl oligopeptidase or prolyl endopeptidase (PREP; EC 3.4.21.26) is an atypical serine protease that hydrolyses peptides and peptide hormones after proline in peptides up to around 30 residues long. Evidence suggests an involvement in learning and memory, and the enzyme is implicated in diseases including amnesia and depression. The first crystal structures determined, of the porcine enzyme, provided direct insight into the mechanisms of substrate size selectivity, substrate specificity, and catalysis. However in these structural studies the enzyme is in a closed state, even in the absence of ligand, leaving questions as to how substrates and products can enter and exit the enclosed central cavity that houses the active site. More recent crystal structures of bacterial PREP have captured the enzyme in an open state, revealing the true extent and nature of the structural dynamics involved, and illuminating an induced fit mode of catalysis and regulation. Molecular modeling has further contributed to our understanding of the conformational changes that occur during catalysis. Here we review the data that has led to our current understanding of the structure and dynamics of this biologically and pharmaceutically important enzyme.
Item Type: | Journal Article | ||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Journal or Publication Title: | CNS & Neurological Disorders - Drug Targets | ||||
Publisher: | Bentham Science Publishers Ltd. | ||||
ISSN: | 1871-5273 | ||||
Official Date: | May 2011 | ||||
Dates: |
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Volume: | Vol.10 | ||||
Number: | No.3 | ||||
Page Range: | pp. 306-310 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access | ||||
Funder: | European Commission (EC) | ||||
Grant number: | HEALTH-F2-2008-223077 (EC) |
Data sourced from Thomson Reuters' Web of Knowledge
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