1OZY

Crystal Structure of Phospholipase A2 (MIPLA3) From Micropechis Ikaheka

1OZY の概要

• エントリーDOI: 10.2210/pdb1ozy/pdb
• 分子名称: PHOSPHOLIPASE A2, SULFATE ION (3 entities in total)
• 機能のキーワード: phospholipase a2, micropechis ikaheka, pancreatic loop, hydrolase
• 由来する生物種: Micropechis ikaheka
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27325.19

構造登録者

Lok, S.M.,Swaminathan, K. (登録日: 2003-04-10, 公開日: 2004-09-28, 最終更新日: 2024-10-16)

主引用文献

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

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: 15720395
DOI: 10.1111/j.1742-4658.2005.04547.x

実験手法

X-RAY DIFFRACTION (2.7 Å)