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|Title:||Structure and function comparison of Micropechis ikaheka snake venom phospholipase A2 isoenzymes||Authors:||Lok, S.-M.
Group IB phospholipase A2
|Issue Date:||Mar-2005||Citation:||Lok, S.-M., Gao, R., Rouault, M., Lambeau, G., Gopalakrishnakone, P., Swaminathan, K. (2005-03). Structure and function comparison of Micropechis ikaheka snake venom phospholipase A2 isoenzymes. FEBS Journal 272 (5) : 1211-1220. ScholarBank@NUS Repository. https://doi.org/10.1111/j.1742-4658.2005.04547.x||Abstract:||Comparison of the crystal structures of three Micropechis ikaheka phospholipase A2 isoenzymes (MiPLA2, MiPLA3 and MiPLA4, which exhibit different levels of pharmacological effects) shows that their C-terminus (residues 110-124) is the most variable. M-Type receptor binding affinity of the isoenzymes has also been investigated and MiPLA4 binds to the rabbit M-type receptor with high affinity. Examination of surface charges of the isoenzymes reveals a trend of increase in positive charges with potency. The isoenzymes are shown to oligomerize in a concentration-dependent manner in a semi-denaturing gel. The C-termini of the medium (MiPLA4) and highly potent (MiPLA2) isoenzyme molecules cluster together, forming a highly exposed area. A BLAST search using the sequence of the most potent MiPLA2 results in high similarity to Staphylococcus aureus clotting factor A and cadherin 11. This might explain the myotoxicity, anticoagulant and hemoglobinuria effects of MiPLA2s. © 2005 FEBS.||Source Title:||FEBS Journal||URI:||http://scholarbank.nus.edu.sg/handle/10635/112653||ISSN:||1742464X||DOI:||10.1111/j.1742-4658.2005.04547.x|
|Appears in Collections:||Staff Publications|
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