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. 2017 Sep;112(9):617–625. doi: 10.1590/0074-02760160522

Fig. 1. : (A) sequence alignment of the inserted regions of the 29 M8 metalloproteases encoded by chromosome 10 of Leishmania (Viannia) braziliensis. The sequence at the top (1LML) corresponds to the only leishmanolysin with the available crystal structure. The sequence alignment was performed using the ALINE program considering the insertion region (magenta box) of leishmanolysin class. Identical and similar residues are represented in black and gray, respectively. The three identified subgroups are colored in blue (DLT/L), red (SSV) and black (NRI); (B) dendogram profile of M8 metalloproteases encoded by chromosome 10 of L. (V.) braziliensis. The dendogram was built employing iTOL server using proteins sequences from geneDB. The numbers on the branches represent the evolutionary distance between different homologous proteins. The three motifs identified are colored and named near the sequence; (C) LbrM.10.0470 structure representing the three-dimensional form of this gene. The catalytic zinc ion is shown as a magenta CPK sphere. The zinc ligands are colored in orange and shown in ball-and-stick representation: His165, His169, and His235. The insertion region is colored orange and the central domain is represented in green. The N and C-terminal domains are represented in red and blue, respectively.

Fig. 1