Structural highlights
Function
PA2A1_OPHHA Snake venom phospholipase A2 (PLA2) that may exhibit cardiotoxicity, myotoxicity, antiplatelet activity, and edema-inducing activity. 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 PubMed
The crystal structure of an acidic phospholipase A(2) from Ophiophagus hannah (king cobra) has been determined by molecular replacement at 2.6-A resolution to a crystallographic R factor of 20.5% (R(free)=23.3%) with reasonable stereochemistry. The venom enzyme contains an unusual "pancreatic loop." The conformation of the loop is well defined and different from those in pancreas PLA(2), showing its structural variability. This analysis provides the first structure of a PLA(2)-type cardiotoxin. The sites related to the cardiotoxic and myotoxic activities are explored and the oligomer observed in the crystalline state is described.
Structure of a cardiotoxic phospholipase A(2) from Ophiophagus hannah with the "pancreatic loop".,Zhang HL, Xu SJ, Wang QY, Song SY, Shu YY, Lin ZJ J Struct Biol. 2002 Jun;138(3):207-15. PMID:12217659[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Huang MZ, Gopalakrishnakone P, Chung MC, Kini RM. Complete amino acid sequence of an acidic, cardiotoxic phospholipase A2 from the venom of Ophiophagus hannah (King Cobra): a novel cobra venom enzyme with "pancreatic loop". Arch Biochem Biophys. 1997 Feb 15;338(2):150-6. PMID:9028866 doi:http://dx.doi.org/S0003-9861(96)99814-8
- ↑ Zhang HL, Xu SJ, Wang QY, Song SY, Shu YY, Lin ZJ. Structure of a cardiotoxic phospholipase A(2) from Ophiophagus hannah with the "pancreatic loop". J Struct Biol. 2002 Jun;138(3):207-15. PMID:12217659
