We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Structure and function comparison ofMicropechis ikahekasnake venom phospholipase A<sub>2</sub> isoenzymes.
- Authors
Lok, Shee-Mei; Gao, Rong; Rouault, Morgane; Lambeau, Gerard; Gopalakrishnakone, Ponnampalam; Swaminathan, Kunchithapadam
- Abstract
Comparison of the crystal structures of threeMicropechis ikahekaphospholipase 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 toStaphylococcus aureusclotting factor A and cadherin 11. This might explain the myotoxicity, anticoagulant and hemoglobinuria effects of MiPLA2s.
- Subjects
VENOM; TOXINS; ISOENZYMES; ENZYMES; HEMOLYTIC anemia; STAPHYLOCOCCUS
- Publication
FEBS Journal, 2005, Vol 272, Issue 5, p1211
- ISSN
1742-464X
- Publication type
Article
- DOI
10.1111/j.1742-4658.2005.04547.x