Figure 1 | Scientific Reports

Figure 1

From: Molecular characterization of HIV-1 Nef and ACOT8 interaction: insights from in silico structural predictions and in vitro functional assays

Figure 1

ACOT8 homology modelling.

(a) Sequence alignment between Acyl-coenzyme A thioesterase 8 (ACOT8_HUMAN) and E. coli thioesterase II (1C8U). â–² indicates aromatic and aliphatic residues (Tyr47, Pro50, Pro90, Leu92) of ACOT8, which are replaced by non-hydrophobic residues in E. coli isoenzyme (Glu, Gly, Ser and Lys respectively). The residues are coloured according to their physico-chemical properties (HKR in cyan, DE in red, STNQ in maroon, AVLIM in pink, FYW in blue, PG in orange and C in green). (b) The modelled ACOT8 dimer (chain A in blue and chain B in brownish). The homology model of ACOT8 was built based on the X-ray structure of the E. coli thioesterase. The two enzymes share about 41% of sequence identity.

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