Abstract

GRADOS TORREZ, Ricardo Enrique. Protein modeling of G. Lamblia Tubulin through sequence homology. Rev.Cs.Farm. y Bioq [online]. 2019, vol.7, n.1, pp.57-66. ISSN 2310-0265.

Abstract Giardiasis caused by Giardia intestina-lis (known as Giardia lamblia), is one of the most common parasitic infections in the world and with a higher prevalence in de-veloping countries like ours. There are many drugs for the treatment of giardiasis, of dif-ferent efficacy and adverse effects such as curcumin that inhibits the polymerization of microtubules by a mechanism other than colchicine. However, the crystallograph-ic structure of G. lamblia Tubulin (a and p chains) remains unknown. The sequence alignment analysis (PBLAST) indicates an identity of 86,98 and 88,32 % between the a and p chains of the Tubulin of G. lamblia and B. taurus (PDB: 5NQT). Homologous Modeling of the protein structure of G. lamblia Tubulin using the B. taurus Tubulin as a template employing the SWISS-MODEL server, generated a protein structure with the fol-lowing parameters: z-core = -1,16 and -1,41, QMEANscore6 = 0,71 and 0,70, % of reli-ability (from Ramachandran plots) = 96,08 y 96,95 %, RMS (Root Mean Square) = 0,081 and MOLPROBITYscore = 1,26. These parameters indicate that the protein structure of G. lamblia Tubulin obtained from Homol-ogy Modeling is of good quality, therefore, this structure could be used in further eval-uations, such as the in silico analysis of anti-Giardia compounds.

Keywords : Protein Modeling; Tubulin; Giardia lamblia; Sequence Homology.

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