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Fig. 2.


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Sequence alignment of GDP-MPs.

A. Multiple sequence alignment of L. infantum, T. thermophilus, and T. maritima GDP-MPs. The L. infantum GDP-MP presents 16.1% and 15.4% of identity with the T. thermophilus and T. maritima, respectively. The signature motif F(V)EKP, essential for the activity of GDP-MPs, is underlined.

B. Multiple sequence alignment of both human and L. infantum GDP-MPs with the protein used as a template for 3D modelling (glucose-1-phosphate thymidylyltransferase from Sulfolobus tokodaii: 2ggo). This alignment shows that L. infantum and human GDP-MPs present 29% and 25% of identity with the template protein, respectively. Both human and leishmanial enzymes share 49% of identity. The amino acids of the template protein active site were identified as described in Materials & Methods. The GDP-MP signature motif F(V)EKP (underlined) is present in both human and leishmanial enzymes, but not in the template protein.

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