1gp7
From Proteopedia
Acidic Phospholipase A2 from venom of Ophiophagus Hannah
Structural highlights
FunctionPA2A1_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 PubMedThe 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 AlsoReferences
| ||||||||||||||||||||
