Abstract
Cathepsin L is a cysteine protease which degrades connective tissue proteins like collagen, elastin and fibronectin. Increase in the expression of cathepsin L in aged kidney leading to considerable loss of organ function in old age. Recently it has been reported that SARS-CoV or SARS-CoV spike protein-pseudotyped retroviruses utilize the enzymatic activity of endosomal cathepsin L protease for viral entry. A 3D structure of rat cathepsin L was constructed in this report through homology modeling using the X-ray structure of procathepsin L from Homo sapiens (PDB code: 1CS8). The homology modeling was done by using the MODELLER 9v2 software. The final model obtained by molecular mechanics and dynamics method and was assessed by PROCHECK and VERIFY 3D graph, which showed that the final refined model is reliable. The model could be further explored for characterizing the protein.
Highlights
Cathepsin L is a member of the papain superfamily of lysosomal cysteine proteases and is one of the most powerful endopeptidases
It was reported that in human SARS-CoV or SARS-CoV spike protein-pseudotyped retroviruses utilize the enzymatic activity of endosomal cathepsin L protease for viral entry (Huang et al, 2006; Li et al, 2006)
It was ascertained that the three-dimensional structure of the protein was not available in Protein Data Bank, the present exercise of developing the 3D model of the rat cathepsin L was undertaken
Summary
Cathepsin L is a member of the papain superfamily of lysosomal cysteine proteases and is one of the most powerful endopeptidases. An effort was made to generate a three-dimensional (3D) model of cathepsin L protein based on the available template crystal structure of procathepsin L from protein data bank (PDB code: 1CS8) (Berman et al, 2000).
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