Type IIA secretory phospholipase A 2 (PLA 2 ) enzymes catalyze the hydrolysis of the sn-2 ester bond of glycerophospholipids to release fatty acids and lysophospholipids. In order to elucidate the role of PLA 2 in inflammatory disorders and to determine the mode of binding of non-steroidal antiinfla
✦ LIBER ✦
Phospholipase A 2 as a Target Protein for Nonsteroidal Anti-Inflammatory Drugs (NSAIDs): Crystal Structure of the Complex Formed between Phospholipase A 2 and Oxyphenbutazone at 1.6 Å Resolution †
✍ Scribed by Singh, Nagendra; Jabeen, Talat; Somvanshi, Rishi K.; Sharma, Sujata; Dey, Sharmistha; Singh, Tej P.
- Book ID
- 127153636
- Publisher
- American Chemical Society
- Year
- 2004
- Tongue
- English
- Weight
- 429 KB
- Volume
- 43
- Category
- Article
- ISSN
- 0006-2960
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## Abstract A novel ligand‐binding site with functional implications has been identified in phospholipase A~2~ (PLA~2~). The binding of non‐steroidal anti‐inflammatory agent indomethacin at this site blocks both catalytic and anti‐coagulant actions of PLA~2~. A group IIA PLA~2~ has been isolated fr