Figure 1.
Panda and dog COMT protein structural simulation.
The simulated panda or dog proteins were indicated with pink color for backbone and red color for special amino acid residues. Human proteins were indicated with blue color for backbone and yellow color for special amino acid residues. The side chain of COMT catecholamine substrate binding sites (Lys144, Asn170, Glu199) and SAM binding sites (Val42, Ser72, Glu90, Asp141) were shown in ball and stick model. (A) The simulated panda COMT structure compared with human COMT. The α4 helix in blue square has turned into a loop in panda. (B) The simulated dog COMT structure compared with human COMT.
Figure 2.
Sequence alignment of COMT from all nine species.
The number for amino acids is based on human soluble COMT. The conserved amino acids were highlighted. The regions for alpha helix and beta sheet were marked at the bottom of the alignment (wave for alpha helix and arrow for beta sheet). The region with missing amino acids in panda is highlighted with purple square box.
Table 1.
Six genes were selected out based on protein structure and sequence consensus percentages.
Table 2.
Seven genes with different Kozak sequence between panda and human.
Figure 3.
Part of the panda COMT 3′UTR and predicted miRNA-199a-5p binding.
COMT 3′UTR secondary structure was predicted by Mfold and part of it was shown on the left. The possible miRNA-199a-5p target with panda COMT gene and the calculated free energy was shown on the right side.