Structural highlights
Function
[PA2B3_BUNCE] Snake venom phospholipase A2 (PLA2) that shows anticoagulant and neurotoxic activities. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides (By similarity).
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
Reinterpretations of the space-group symmetry are reported for two crystal structures of phospholipase A(2) isoforms (PDB codes 1u4j and 1g2x). The two structures reported in space groups R3 and C2 are isomorphous with a third isoform with space group R32 (PDB code 1fe5). The original structure reports were interpreted in terms of different oligomeric forms of the isoforms, but these conclusions are not supported by the isomorphous structures.
An alternate description of two crystal structures of phospholipase A2 from Bungarus caeruleus.,Le Trong I, Stenkamp RE Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):548-9. Epub 2007, Mar 16. PMID:17372360[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Le Trong I, Stenkamp RE. An alternate description of two crystal structures of phospholipase A2 from Bungarus caeruleus. Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):548-9. Epub 2007, Mar 16. PMID:17372360 doi:10.1107/S0907444907007354
