2i0u
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Crystal structures of phospholipases A2 from Vipera nikolskii venom revealing Triton X-100 bound in hydrophobic channel
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Structural highlights
FunctionPA2B1_VIPNI Heterodimer: shows the same activities as the monomer, but with a lower potency. Monomer: snake venom phospholipase A2 (PLA2) that shows presynaptic neurotoxicity, anticoagulant activity and that weakly inhibits ADP-induced platelet aggregation (PubMed:18083205). Inhibits exocytosis in pancreatic beta cells, confirming it can act presynaptically in inhibiting the exocytosis of neurotransmitters in neurons (PubMed:19500614). PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.[1] [2] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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This page was last modified 08:10, 30 October 2024.