Understanding the structure and function of Plasmodium aminopeptidases to facilitate drug discovery.
Journal
Current opinion in structural biology
ISSN: 1879-033X
Titre abrégé: Curr Opin Struct Biol
Pays: England
ID NLM: 9107784
Informations de publication
Date de publication:
10 2023
10 2023
Historique:
received:
31
03
2023
revised:
01
08
2023
accepted:
03
08
2023
medline:
18
9
2023
pubmed:
2
9
2023
entrez:
1
9
2023
Statut:
ppublish
Résumé
Malaria continues to be the most widespread parasitic disease affecting humans globally. As parasites develop drug resistance at an alarming pace, it has become crucial to identify novel drug targets. Over the last decade, the metalloaminopeptidases have gained importance as potential targets for new antimalarials. These enzymes are responsible for removing the N-terminal amino acids from proteins and peptides, and their restricted specificities suggest that many perform unique and essential roles within the malaria parasite. This mini-review focuses on the recent progress in structure and functional data relating to the Plasmodium metalloaminopeptidases that have been validated or shown promise as new antimalarial drug targets.
Identifiants
pubmed: 37657352
pii: S0959-440X(23)00167-7
doi: 10.1016/j.sbi.2023.102693
pii:
doi:
Substances chimiques
Aminopeptidases
EC 3.4.11.-
Folic Acid Antagonists
0
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
102693Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier Ltd.. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.