• Interaction

    AccNo. 58300 Score 0.49
    Name PM_20575133
    Kd 1.0

    Peptide

    AccNo. 58183
    Name YYPVY
    Sequence YYPVY
    58183_small
    Internalized no
    Is Motif no

    Interactor

    AccNo. 57694
    Name unknown

    Experiment

    AccNo. 58109
    Classification incorrect?
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    Voting_motivation
    CA CVD DM APO ANG MI BD
    0.70 0.59 0.31 0.99 0.53 0.14 0.41 Vote
    plus plus plus plus plus plus plus Yes
    minus minus minus minus minus minus minus No
    Name PM_20575133
    Detection unspecified method, MI:0686
    Source Pubmed Text Id 20575133
    Journal Chembiochem. 2010 Jul 26;11(11):1594-9.
    Title A novel cyanobacterial nostocyclopeptide is a potent antitoxin against microcystins.
    Authors Jokela J, Herfindal L, Wahlsten M, Permi P, Selheim F, Vasconçelos V, Døskeland SO, Sivonen K
    Text Cyanobacterial hepatotoxins (microcystins and nodularins) cause numerous animal poisonings worldwide each year and are threats to human health. However, we found that extracts from several cyanobacteria isolates failed to induce hepatotoxicity even if they contained high concentrations of the liver toxin microcystin. The antitoxic activity abolishes all morphological hallmarks of microcystin-induced apoptosis, and therefore invalidates cell-based assays of the microcystin content of bloom-forming cyanobacteria. The antitoxin was purified from a cyanobacterial isolate (Nostoc sp. XSPORK 13A) from the Baltic Sea, and the activity was shown to reside in a novel cyclic peptide of the nostocyclopeptide family (nostocyclopeptide M1, Ncp-M1) that consists of seven amino acids (Tyr1-Tyr2-D-HSe3-L-Pro4-L-Val5-(2S,4S)-4-MPr6-Tyr7; MW=881) with an imino linkage between Tyr1 and Tyr7. Ncp-M1 did not compete with labelled microcystin for binding to protein phosphatase 2A; this explains why the antitoxin did not interfere with phosphatase-based microcystin assays. Currently used agents that interfere with microcystin action, such as inhibitors of ROS formation, microcystin uptake and Cam-kinase activity, are themselves inherently toxic. Since Ncp-M1 is potent and nontoxic it promises to become a useful mechanistic tool as soon as its exact cellular target is elucidated.
    Mesh Terms Antitoxins/chemistry; Antitoxins/isolation & purification; Carcinogens; Cyanobacteria/chemistry; Microcystins/antagonists & inhibitors; Peptides, Cyclic/isolation & purification; Peptides, Cyclic/pharmacology; Structure-Activity Relationship
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