2a94
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(New page: 200px<br /><applet load="2a94" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a94, resolution 1.500Å" /> '''Structure of Plasmo...)
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Revision as of 05:52, 21 November 2007
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Structure of Plasmodium falciparum lactate dehydrogenase complexed to APADH.
Overview
Malaria caused by Plasmodium vivax is a major cause of global morbidity, and, in rare cases, mortality. Lactate dehydrogenase is an essential, Plasmodium protein and, therefore, a potential antimalarial drug target., Ideally, drugs directed against this target would be effective against, both major species of Plasmodium, P. falciparum and P. vivax. In this, study, the crystal structure of the lactate dehydrogenase protein from P., vivax has been solved and is compared to the equivalent structure from the, P. falciparum enzyme. The active sites and cofactor binding pockets of, both enzymes are found to be highly similar and differentiate these, enzymes from their human counterparts. These structures suggest effective, inhibition of both enzymes should be readily achievable with a common, inhibitor. The crystal structures of both enzymes have also been solved in, complex with the synthetic cofactor APADH. The unusual cofactor binding, site in these Plasmodium enzymes is found to readily accommodate both NADH, and APADH, explaining why the Plasmodium enzymes retain enzymatic activity, in the presence of this synthetic cofactor.
About this Structure
2A94 is a Single protein structure of sequence from Plasmodium falciparum with AP0 as ligand. Active as L-lactate dehydrogenase, with EC number 1.1.1.27 Full crystallographic information is available from OCA.
Reference
Structure of lactate dehydrogenase from Plasmodium vivax: complexes with NADH and APADH., Chaikuad A, Fairweather V, Conners R, Joseph-Horne T, Turgut-Balik D, Brady RL, Biochemistry. 2005 Dec 13;44(49):16221-8. PMID:16331982
Page seeded by OCA on Wed Nov 21 07:59:36 2007
