Conserved Domains, Residues, WebLogo and Active Sites of Caspase-Cascades Related to Apoptotic Signaling Pathway
Chiranjib Chakraborty, Jinny Tomar and V.K. Gera
AbstractCaspases belong to the family of cysteinyl aspartate–a specific proteases which control the programmed cell death process, or apoptosis. In this paper, we have performed a structural bioinformatics analysis of the conserved domains and residues, WebLogo generation and active sites identification related to apoptosis activator and apoptosis executioner caspase-cascades. Here, we have also shown conservation patterns of backbone structures of activator and executioner caspase-cascades. It has been noted that the numbers of highly conserved amino acid residues are very high in caspase-12 (36 aa) and low in caspase-7 (18 aa). We have observed that highly conserved amino acids residues like LYS154, PRO155, LYS156 are present in caspase-3 and caspase-6. In apoptosis and executioner caspases, these amino acids may play an active role. From WebLogo, it has been observed that the stack height is very low between the sequences 231 to 240; 2.3 bits stack height has been observed in 1st sequence position and 236th position where WebLogo stack height is very low. We have identified 10 active sites in caspase-3, caspase-6, caspase-7 which may be helpful in drug development using caspase-cascades. Here, we have also performed literature survey about the drug development using caspase-cascades.
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