Resumo

PATINO-GONZALEZ, Edwin; PATINO-MARQUEZ, Isabel Andrea  e  ALZATE, Juan Fernando. Crystallization and prediction of three-dimensional structure of the homologue protein of the receptor for activated c-kinase (lack) from leishmania. Rev.Colomb.Quim. [online]. 2014, vol.43, n.3, pp.17-23. ISSN 0120-2804.

Leishamnia parasites are the causative agents of the leishmaniasis disease. Due to its broad distribution, parasites are endemic in approximately 98 countries. Twenty species of Leishmaniasp has been described as human pathogens and several of them present different clinical manifestations. This feature poses a significant challenge to the general goals of parasite control and erradication. There is no a protective vaccine for humans, despite substantial efforts by many research teams. Alternatives to discover new drugs are based on the design of new compounds that bind selected targets. Mainly, the targets are proteins involved in key metabolic or cellular processes of the pathogen, e.g. parasitization of vertebrate host cells. The efficient parasitization of the vertebrate host by Leishmania parasites depends on the expression of different molecules including Lack protein. The knockout parasites fail to survive inside the vertebrate host cells. In this article we highlight the conditions to perform the refold, purification, and crystallizing of the Lack protein of the human pathogen Leishmania (Viannia) panamensis. Moreover, we present structure modelling analysis which shows a protein conformation like a fan organized in 7 blades, each one composed of 4 b sheets. Furthermore, the structure of Lack protein was found to be similar to RACK1-ribosome associated protein from Trypanosoma brucei and Saccharomyces cerevisiae and other eukaryotes. The structural characteristics of Lack protein could be used for exploration of new drugs.

Palavras-chave : Crystallization; Lack; Leishmania; refolding; structure.

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