1ozy
From Proteopedia
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| , resolution 2.70Å | |||||||
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| Ligands: | |||||||
| Activity: | Phospholipase A(2), with EC number 3.1.1.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 30 22:52:46 2008
