Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/14419
Title: Structural comparison of Micropechis ikaheka phospholipase A2 isoenzymes reveals a pharmacological motif on the C-terminus
Authors: LOK SHEE MEI
Keywords: phospholipase A2, structure, pharmacological motif, c-terminus, multimerization, Micropechis ikaheka
Issue Date: 28-Feb-2005
Source: LOK SHEE MEI (2005-02-28). Structural comparison of Micropechis ikaheka phospholipase A2 isoenzymes reveals a pharmacological motif on the C-terminus. ScholarBank@NUS Repository.
Abstract: Comparison of three Micropechis ikaheka phospholipase A2 isoenzymes (MiPLA2, MiPLA3 and MiPLA4) crystal structures showed that the C-termini are the most variable. Several evidences point to the C-terminal as pharmacologically important. This region has been documented to be highly variable and yet the two most potent isoenzymes have similar sequences. MiPLA4, which has high affinity to the rabbit M-type receptor, also has unique residues at this region. Increased in positive charges on the C-terminal face with the isoenzyme potency was observed. The isoenzmyes were shown to be able to oligomerize in a concentration dependent manner. As a result of multimerization, the molecules of MiPLA2 and MiPLA4 clustered all C-termini forming a highly exposed area commonly observed in other receptor binding sites. Finally, the most potent MiPLA2 C-terminus sequence is similar to the Staphylococcus aureus clotting factor A, hemoglobin a-chain and cadherin 11 molecules and they may explain for its myotoxicity, anticoagulant and hemoglobinuria effects.
URI: http://scholarbank.nus.edu.sg/handle/10635/14419
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