1OZY
Crystal Structure of Phospholipase A2 (MIPLA3) From Micropechis Ikaheka
Summary for 1OZY
| Entry DOI | 10.2210/pdb1ozy/pdb |
| Descriptor | PHOSPHOLIPASE A2, SULFATE ION (3 entities in total) |
| Functional Keywords | phospholipase a2, micropechis ikaheka, pancreatic loop, hydrolase |
| Biological source | Micropechis ikaheka |
| Total number of polymer chains | 2 |
| Total formula weight | 27325.19 |
| Authors | Lok, S.M.,Swaminathan, K. (deposition date: 2003-04-10, release date: 2004-09-28, Last modification date: 2024-10-16) |
| Primary citation | Lok, S.M.,Gao, R.,Rouault, M.,Lambeau, G.,Gopalakrishnakone, P.,Swaminathan, K. Structure and function comparison of Micropechis ikaheka snake venom phospholipase A2 isoenzymes FEBS J., 272:1211-1220, 2005 Cited by PubMed 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. PubMed: 15720395DOI: 10.1111/j.1742-4658.2005.04547.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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