1y4l
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(New page: 200px<br /><applet load="1y4l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y4l, resolution 1.70Å" /> '''Crystal structure of...)
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Revision as of 04:26, 21 November 2007
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Crystal structure of Bothrops asper myotoxin II complexed with the anti-trypanosomal drug suramin
Overview
Suramin, a synthetic polysulfonated compound, developed initially for the, treatment of African trypanosomiasis and onchocerciasis, is currently used, for the treatment of several medically relevant disorders. Suramin, heparin, and other polyanions inhibit the myotoxic activity of Lys49, phospholipase A2 analogues both in vitro and in vivo, and are thus of, potential importance as therapeutic agents in the treatment of viperid, snake bites. Due to its conformational flexibility around the single bonds, that link the central phenyl rings to the secondary amide backbone, the, symmetrical suramin molecule binds by an induced-fit mechanism, complementing the hydrophobic surfaces of the dimer and adopts a novel, conformation that lacks C2 symmetry in the dimeric crystal structure of, the suramin-Bothrops asper myotoxin II complex. The simultaneous binding, of suramin at the surfaces of the two monomers partially restricts access, to the nominal active sites and significantly changes the overall charge, of the interfacial recognition face of the protein, resulting in the, inhibition of myotoxicity.
About this Structure
1Y4L is a Single protein structure of sequence from Bothrops asper with SVR, P33 and IPA as ligands. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.
Reference
Inhibition of myotoxic activity of Bothrops asper myotoxin II by the anti-trypanosomal drug suramin., Murakami MT, Arruda EZ, Melo PA, Martinez AB, Calil-Elias S, Tomaz MA, Lomonte B, Gutierrez JM, Arni RK, J Mol Biol. 2005 Jul 15;350(3):416-26. PMID:15961104
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