3O4M

Crystal structure of porcine pancreatic phospholipase A2 in complex with 1,2-dihydroxybenzene

Summary for 3O4M

• Entry DOI: 10.2210/pdb3o4m/pdb
• Related: 2B00 2B03 2B04 3HSW 3L30 3L69
• Descriptor: Phospholipase A2, major isoenzyme, CALCIUM ION, CATECHOL, ... (4 entities in total)
• Functional Keywords: catechol binding, pla2, pancreatic enzyme, disulfide bond, lipid degradation, lipoprotein, metal-binding, palmitate, pyrrolidone carboxylic acid, pancreas, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Sus scrofa (Pig)
• Cellular location: Secreted: P00592
• Total number of polymer chains: 1
• Total formula weight: 14199.98

Authors

Dileep, K.V.,Tintu, I.,Karthe, P.,Mandal, P.K.,Haridas, M.,Sadasivan, C. (deposition date: 2010-07-27, release date: 2010-08-25, Last modification date: 2024-10-30)

Primary citation

Dileep, K.V.,Tintu, I.,Mandal, P.K.,Karthe, P.,Haridas, M.,Sadasivan, C.
Binding to PLA(2) may contribute to the anti-inflammatory activity of catechol
Chem.Biol.Drug Des., 2011

PubMed Abstract: Inhibiting PLA(2) activity should, in theory, be an effective approach to control the inflammation. Several naturally occurring polyphenolic compounds have been reported as inhibitors of PLA(2) . Among the naturally occurring polyphenols, catechol (1,2-dihydroxybenzene) possesses anti-inflammatory activity. Catechol can inhibit cyclooxygenase and lipo-oxygenase. By means of enzyme kinetic study, it was revealed that catechol can inhibit PLA(2) also. Crystal structure showed that catechol binds to PLA(2) at the opening of the active site cleft. This might stop the entry of substrate into the active site. Hence, catechol can be used as a lead compound for the development of novel anti-inflammatory drugs with PLA(2) as the target.

PubMed: 21995306
DOI: 10.1111/j.1747-0285.2011.01258.x

Experimental method

X-RAY DIFFRACTION (2.5 Å)