1ozy
From Proteopedia
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Crystal Structure of Phospholipase A2 (MIPLA3) From Micropechis Ikaheka
Overview
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.
About this Structure
1OZY is a Protein complex structure of sequences from Micropechis ikaheka with SO4 as ligand. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.
Reference
Structure and function comparison of Micropechis ikaheka snake venom phospholipase A2 isoenzymes., Lok SM, Gao R, Rouault M, Lambeau G, Gopalakrishnakone P, Swaminathan K, FEBS J. 2005 Mar;272(5):1211-20. PMID:15720395
Page seeded by OCA on Sun Nov 25 01:44:42 2007
