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 ✦
Aspirin induces its anti-inflammatory effects through its specific binding to phospholipase A 2 : Crystal structure of the complex formed between phospholipase A 2 and aspirin at 1.9 Å resolution
✍ Scribed by Singh, Rajendra Kumar; Ethayathulla, A.S.; Jabeen, Talat; Sharma, Sujata; Kaur, Punit; Singh, Tej P.
- Book ID
- 118167597
- Publisher
- Informa plc
- Year
- 2005
- Tongue
- English
- Weight
- 446 KB
- Volume
- 13
- Category
- Article
- ISSN
- 1061-186X
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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