4.4 Sequence scanning of Rv2615c protein
Predictions of I-TASSER strongly suggested the similarity of Rv2615c
with APAF1-apoptosome structure involved in Caspase activation and cell
death pathways followed by in-vitro experiments which further
confirmed the apoptogenic role played by Rv2615c protein. It is reported
that the APAF1-apoptosome activates the Caspase9 via CARD-CARD
interaction between APAF1-Caspase9. Therefore, multiple sequence
alignment of Rv2615c was performed with CARD-APAF1 and CARD-Caspase9.
The alignment was checked for various conserved and similar residues.
Secondary structure of predicted CARD-like domain in Rv2615c was
analysed with MINNOU server (Cao et al. , 2006). Structural
superimposition of predicted CARD-like domain in Rv2615c with CARD-APAF1
and CARD-Caspase9 was carried out in Pymol software.