1poa

Structural highlights

Function

PA2A1_NAJAT Snake venom phospholipase A2 (PLA2) that has high affinity for muscarinic acetylcholine receptors mAChRs (CHRM) and has the ability to activate them. In guinea-pig ileum, produces an onset and dose-dependent contraction. Has also weak anticoagulant activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.^{[1] [2]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Phospholipase A2 3D structures

References

1. ↑ Huang LF, Zheng JB, Xu Y, Song HT, Yu CX. A snake venom phospholipase A2 with high affinity for muscarinic acetylcholine receptors acts on guinea pig ileum. Toxicon. 2008 May;51(6):1008-16. doi: 10.1016/j.toxicon.2008.01.006. Epub 2008, Jan 17. PMID:18281071 doi:http://dx.doi.org/10.1016/j.toxicon.2008.01.006
2. ↑ Kini RM, Evans HJ. Structure-function relationships of phospholipases. The anticoagulant region of phospholipases A2. J Biol Chem. 1987 Oct 25;262(30):14402-7. PMID:3117784