6al3
From Proteopedia
Lys49 PLA2 BPII derived from the venom of Protobothrops flavoviridis.
Structural highlights
FunctionPA2B2_PROFL Snake venom phospholipase A2 (PLA2) that shows anticoagulant activities, strong myolytic activity, infiltration of polymorphonuclear cells, and edema in stromal tissues. Induces cell death of Jurkat cells in a concentration dependent manner. Shows a low phospholipase A2 activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.[1] [2] Publication Abstract from PubMedPhospholipase A2 (PLA2) is one of the representative toxic components of snake venom. PLA2s are categorized into several subgroups according to the amino acid at position 49, which comprises either Asp49, Lys49, Arg49 or Ser49. Previous studies suggested that the Lys49-PLA2 assembles into an extremely stable dimer. Although the behavior on Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing or non-reducing conditions suggested the presence of intermolecular disulfide bonds, these bonds were not observed in the crystal structure of Lys49-PLA2. The reason for this discrepancy between the crystal structure and SDS-PAGE of Lys49-PLA2 remains unknown. In this study, we analyzed a Lys49-PLA2 homologue from Protobothrops flavoviridis (PflLys49-PLA2 BPII), by biophysical analyses including X-ray crystallography, SDS-PAGE, native-mass spectrometry, and analytical ultracentrifugation. The results demonstrated that PflLys49-PLA2 BPII spontaneously oligomerized in the presence of SDS, which is one of the strongest protein denaturants. SDS-induced oligomerization of Lys49-phospholipase A2 from snake venom.,Matsui T, Kamata S, Ishii K, Maruno T, Ghanem N, Uchiyama S, Kato K, Suzuki A, Oda-Ueda N, Ogawa T, Tanaka Y Sci Rep. 2019 Feb 20;9(1):2330. doi: 10.1038/s41598-019-38861-8. PMID:30787342[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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