Application | Comment | Organism |
---|---|---|
drug development | applicability of minocycline as a lead compound for the design of specific inhibitors of PLA2, which play a crucial role in inflammatory processes | Naja naja |
Crystallization (Comment) | Organism |
---|---|
PLA2 in complex with inhibitor minocycline, by hanging drop vapor diffusion method, at 1.65 A resolution. Belongs to space group P213 with unit cell parameters a = 68.712 A, b = 68.712 A, c = 68.712 A. Minocycline binds to the hydrophobic cleft at the entrance of the active site of PLA2. As a consequence, the access of substrate molecules to the active site is blocked, and the conformation of the Ca2+-binding loop is stabilized in the Ca2+-free conformation of the apo-enzyme, thus resulting in inhibition of enzymatic activity. Interaction between PLA2 and minocycline is mainly hydrophobic | Naja naja |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
minocycline | interferes with the conformation of the active-site Ca2+-binding loop, preventing Ca2+ binding, and shields the active site from substrate entrance, resulting in inhibition of the enzyme. Dissociation constant for PLA2 is Kd = 0.00018 M | Naja naja |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | Ca2+ is coordinated by the Asp48 carboxylate, two water molecules, and three polypeptide carbonyl oxygen atoms of the Ca2+-binding loop | Naja naja |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Naja naja | P15445 | - |
- |
Purification (Comment) | Organism |
---|---|
by centrifugation and on anion-exchange column | Naja naja |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
venom | - |
Naja naja | - |
Subunits | Comment | Organism |
---|---|---|
trimer | crystallography | Naja naja |
Synonyms | Comment | Organism |
---|---|---|
PLA2 | - |
Naja naja |
secretory phospholipase A2 | - |
Naja naja |