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dc.contributor.authorCaterina Peggion
dc.contributor.authorFiorella Tonello
dc.contributor.otherDepartment of Biomedical Sciences, University of Padova, Via U. Bassi, 58/B, 35131 Padova, Italy
dc.contributor.otherCNR of Italy, Neuroscience Institute, viale G. Colombo 3, 35131 Padova, Italy
dc.date.accessioned2025-10-09T05:27:16Z
dc.date.available2025-10-09T05:27:16Z
dc.date.issued01-04-2021
dc.identifier.urihttps://www.mdpi.com/2072-6651/13/4/290
dc.identifier.urihttp://digilib.fisipol.ugm.ac.id/repo/handle/15717717/41033
dc.description.abstractSnake venom phospholipases A2 (PLA2s) have sequences and structures very similar to those of mammalian group I and II secretory PLA2s, but they possess many toxic properties, ranging from the inhibition of coagulation to the blockage of nerve transmission, and the induction of muscle necrosis. The biological properties of these proteins are not only due to their enzymatic activity, but also to protein–protein interactions which are still unidentified. Here, we compare sequence alignments of snake venom and mammalian PLA2s, grouped according to their structure and biological activity, looking for differences that can justify their different behavior. This bioinformatics analysis has evidenced three distinct regions, two central and one C-terminal, having amino acid compositions that distinguish the different categories of PLA2s. In these regions, we identified short linear motifs (SLiMs), peptide modules involved in protein–protein interactions, conserved in mammalian and not in snake venom PLA2s, or vice versa. The different content in the SLiMs of snake venom with respect to mammalian PLA2s may result in the formation of protein membrane complexes having a toxic activity, or in the formation of complexes whose activity cannot be blocked due to the lack of switches in the toxic PLA2s, as the motif recognized by the prolyl isomerase Pin1.
dc.language.isoEN
dc.publisherMDPI AG
dc.subject.lccMedicine
dc.titleShort Linear Motifs Characterizing Snake Venom and Mammalian Phospholipases A2
dc.typeArticle
dc.description.keywordssnake venom phospholipases A2
dc.description.keywordsneurotoxins
dc.description.keywordsmyotoxins
dc.description.keywordssecretory phospholipases A2
dc.description.keywordsPLA2G1B
dc.description.keywordsPLA2G2A
dc.description.doi10.3390/toxins13040290
dc.title.journalToxins
dc.identifier.e-issn2072-6651
dc.identifier.oaioai:doaj.org/journal:43e37319ce8d46ec8c21df0dc9ae248f
dc.journal.infoVolume 13, Issue 4


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