1psj | pdb_00001psj
ACIDIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS
Structural highlights
FunctionPA2A_GLOHA Snake venom phospholipase A2 (PLA2) that acts in vivo as an anti-thrombotic agent. Inhibits platelet aggregation induced by ADP, arachidonic acid, and thrombin. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of acidic phospholipase A2 from the venom of Agkistrodon halys pallas has been determined by molecular replacement at 2.0 A resolution to a crystallographic R-factor of 0.157. The overall structure of the molecule is very similar to those of other phospholipase A2 species of known structure. The catalytic site, the hydrophobic channel and the N-terminal region show greatest structural conservation. The Ca(2+)-binding region has a conformation that resembles closely that of bovine PLA2 rather than Crotalus atrox PLA2. Compared with other PLA2 species, the conformation of the C-terminal ridge shows significant difference due to the insertion of two residues. A unique aromatic patch appears on one face of the molecules, surrounded by two acidic residues, the relevant features of this structure and their possible biological implications are discussed. Crystal structure of an acidic phospholipase A2 from the venom of Agkistrodon halys pallas at 2.0 A resolution.,Wang XQ, Yang J, Gui LL, Lin ZJ, Chen YC, Zhou YC J Mol Biol. 1996 Feb 9;255(5):669-76. PMID:8636969[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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