The control of extracellular nucleoside concentrations by Nucleoside Triphosphate Diphosphohydrolase (NTPDase) is essential in the regulation of the purinergic signalling and also in immune response. In humans, eight members (HsNTPDase) were identified as transmembrane and secreted proteins. In
, the causative agent of schistosomiasis, NTPDases similar to the humans enzymes have also been identified. The expression of these enzymes in
(SmATPDases) is related to the weakening of the immune and inflammatory responses of the host against infections. Despite of the high phylogenetic conservation between these proteins, SmATPDases have been reported as molecular target candidates for antischistosomal treatment. In this work, we constructed three-dimensional models for secreted SmATPDase and HsNTPDase6, using comparative modeling technique. The comparative structural analysis aim the investigation of possible differences that could help future works in the development of new therapies that minimize the risk of cross inhibition.
Bitte loggen Sie sich ein, um Zugang zu diesem Inhalt zu erhalten