Structural highlights
Function[PA2A_DEIAC] Snake venom phospholipase A2 (PLA2) that inhibits ADP-induced platelet aggregation. 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 PubMedAn acidic phospholipase A(2) was purified from Deinagkistrodon acutus (Agkistrodon acutus) which displays an inhibitory effect on platelet aggregation. The three-dimensional structure of the enzyme was determined by molecular replacement at 2.6 A resolution with a crystallographic R factor of 18.40% (R(free) = 22.50%) and reasonable stereochemistry. Two molecules in the asymmetric unit form a dimer and the dimer formation accompanies a significant conformational adaptation of segment 14-23, a constituent of the 'interface recognition site' (IRS). This probably reflects the inherent structural flexibility of the IRS. The possible expansion of the site for inhibiting platelet aggregation as proposed previously [Wang et al. (1996), J. Mol. Biol. 255, 669-676] is discussed. Structure of an acidic phospholipase A2 from the venom of Deinagkistrodon acutus.,Gu L, Zhang H, Song S, Zhou Y, Lin Z Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):104-10. Epub 2001, Dec 21. PMID:11752784[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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