Structural Modeling of Toxoplasma gondii TGME49_289620 Proteinase

  • Mateo Murillo León
  • Diego Mauricio Moncada Giraldo
  • Diego Alejandro Molina
  • Aylan Farid Arenas
  • Jorge Enrique Gómez
Part of the Advances in Intelligent Systems and Computing book series (AISC, volume 232)

Abstract

Cysteine proteinases play key roles in host-parasite interactions, including host invasion, parasite differentiation, and intracellular survival. Toxoplasma gondii expresses five cysteine proteases, including one cathepsin L‑like (TgCPL), one cathepsin B‑like (TgCPB) and three cathepsin C‑like (TgCPC1, 2 and 3) proteases. We performed the Structural modeling of catalytic domain of TgCPC1 with server I-TASSER, the template selected for homology modeling was Dipeptidyl peptidase I (Cathepsin C) (PDB code: 1JQP). The C-Score of structural modeling of catalytic domain was -0.5; in the L-domain there are nine ɑ-helices and two β-strands and in the right domain there are four β-strands and two ɑ-helices. Cys-440, His-651 and Asn-676, form the cysteine protease catalytic triad in the active site. Adjacent to active site there is a Tyr441 this residue may be involved in the binding of the N terminus of the peptide substrate. A tyrosine residue (Tyr 578) that binds a chloride ion in the crystal structures of rat and human Cathepsin C is also conserved.

Keywords

cathepsin structural modeling Toxoplasma gondii protease 

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Copyright information

© Springer International Publishing Switzerland 2014

Authors and Affiliations

  • Mateo Murillo León
    • 1
  • Diego Mauricio Moncada Giraldo
    • 1
  • Diego Alejandro Molina
    • 1
  • Aylan Farid Arenas
    • 1
  • Jorge Enrique Gómez
    • 1
  1. 1.Grupo de Estudio en Parasitología Molecular (GEPAMOL)ArmeniaColombia

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