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. 2016 Jun 16;3:262. Originally published 2014 Oct 31. [Version 3] doi: 10.12688/f1000research.5145.3

Figure 4. Non-specific binding of suramin to phospholipase A2-like proteins (PLA2).

Figure 4.

( a) MSA of three PLA2 from poisonous vipers: (i) PLA2-X, PDBid:1Y4L from Bothrops asper, (ii) PLA2-Y, PDBid:3BJW from Echis carinatus and (iii) PLA2-Z, PDBid:4YV5 from Bothrops moojeni shows that PLA2-Y is significantly different from the other two proteins in the charge composition of the residues. For example, the positively charged Lys53 which makes contact with suramin in PLA2-X, and is conserved in PLA2-Z, is replaced by the negatively charged Asp53 in PLA2-Y.( b) The DOCLASP docked suramin to PLA2-Z based on the binding residues obtained from PLA2-X (Lys53, Lys69 and Tyr52) shows that there are two possible binding sites of suramin within PLA2-X/Z.