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Year : 2011  |  Volume : 2  |  Issue : 3  |  Page : 28  

Identification, sequence and structural analysis of cathepsin L - like proteins in Drosophila melanogaster


1 Institute of Life Sciences, Nalco Square, Bhubaneswar 751023, India
2 Sam Higginbottom Institute of Agriculture, Technology and Sciences, Allahabad 211007, India
3 Cancer Research Technology Ltd., Birkbeck College, University of London, London, WC1E 7HX, United Kingdom
4 Department of Zoology, Berhampur University, Berhampur 760 007, India
5 European Molecular Biology Laboratory, 6 Rue Jules Horowitz, 38042 Grenoble CEDEX 9, France

Date of Web Publication26-May-2012

Correspondence Address:
Sunil Kumar
Institute of Life Sciences, Nalco Square, Bhubaneswar 751023
India
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Source of Support: None, Conflict of Interest: None


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How to cite this article:
Kumar S, Farmer R, Turnbull AP, Tripathy NK, Manjasetty BA. Identification, sequence and structural analysis of cathepsin L - like proteins in Drosophila melanogaster. J Nat Sc Biol Med 2011;2, Suppl S1:28

How to cite this URL:
Kumar S, Farmer R, Turnbull AP, Tripathy NK, Manjasetty BA. Identification, sequence and structural analysis of cathepsin L - like proteins in Drosophila melanogaster. J Nat Sc Biol Med [serial online] 2011 [cited 2020 Jan 28];2, Suppl S1:28. Available from: http://www.jnsbm.org/text.asp?2011/2/3/28/95744

Sequencing genome projects have led to a dramatic increase in the number of publicly available DNA and protein sequences. Meticulous use of bioinformatics tools has helped the biology community to identify the 'starting points' for further studies using experimental techniques. Of the model organisms sequenced, the Drosophila genome has provided a powerful resource to study proteins that are related to proteins of known function in other organisms. In this present study, five well characterized Cathepsin-L proteins from different arthropods were used as query sequences for the Drosophila genome database. Cathepsin-L is a cysteine protease which degrades connective tissue proteins including collagen, elastin and fibronectin. A search yielded 10 Cathepsin-L like sequences, of which eight putatively represent novel Cathepsin-L like proteins. To understand the phylogenetic relationship among these cathepsin-L like proteins, a phylogenetic tree was constructed based on their sequences. Models of the tertiary structures of Cathepsin-L were constructed using homology modelling methods and subjected to molecular dynamics simulations in order to explore the conservation of their protein folds and the architecture of their active site clefts Our findings show that all of the potential Drosophila cathepsin L-like proteins contain at least one cathepsin propeptide inhibitor domain. Multiple sequence alignments clearly indicate that amino acid residues critical for inhibitor binding are conserved. Molecular dynamics studies of the predicted models clearly indicate that the protein fold is conserved and provide information relating to the active site cleft of Cathepsin L. Further validation of these modelling studies could include the amplification of the cDNAs of the putative cathepsin-L proteins, followed by their over-expression, purification and activity measurements to confirm that they are indeed cathepsin-L like proteins.




 

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