Lipophosphoglycan 3 From Leishmania infantum chagasi Binds Heparin With Micromolar Affinity.

In this study, we identified the product with an HSP90 (heat shock protein 90) domain encoded by lipophosphoglycan (LPG3) gene as a L infantum chagasi HBP (HBPLc). Structural analysis using the LPG3 recombinant protein suggests that it is organized as a tetramer. Binding analysis confirms that it is capable of binding heparin with micromolar affinity. Inhibition of adenosine triphosphatase activity in the presence of heparin, molecular modeling, and in silico docking analysis suggests that heparin-binding site superimposes with the adenosine triphosphate-binding site. Together, these results show new properties of LPG3 and suggest an important role in leishmaniasis.
PMID: 29568220 [PubMed]

Source: Bioinformatics and Biology Insights - March 27, 2018 Category: Bioinformatics Authors: Martins TVF, Zeraik AE, Alves NO, de Oliveira LL, de Oliveira Mendes TA, DeMarco R, de Almeida Marques-da-Silva E Tags: Bioinform Biol Insights Source Type: research