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In-Silico Structural & Molecular Characterization Of Clgr From Mycobacterium Tuberculosis
| Content Provider | Semantic Scholar |
|---|---|
| Author | Joshi, Yogesh N. Salunkhe, Rupali D. |
| Copyright Year | 2018 |
| Abstract | Tuberculosis (TB), caused by Mycobacterium tuberculosis (Mtb), is the leading cause of death from an infectious disease worldwide. Chaperone and protease systems play essential roles in cellular homeostasis and have vital functions in controlling the abundance of specific cellular proteins involved in processes such as transcription, replication, metabolism and virulence. Bacteria have evolved accurate regulatory systems to control the expression and function of chaperones and potentially destructive proteases. ClgR performs different functions during stress response and is important for the pathogenicity of Mtb. Clp protease plays an unusual and essential role in Mtb and may serve as an ideal target for antimycobacterial therapy. Mtb encodes two ClpP genes, ClpP1 and ClpP2, which associate together to form a single proteolytic complex, referred to as ClpP1P2. ClgR regulation of chaperone and protease system is essential for mycobacterium tuberculosis parasitism of the microphages. Clp protease complex is an attractive novel target for antitubercular drugs because it is essential for growth and virulence. The present investigation includes retrieval of amino acid information and sequence analysis of ClgR from major protein sequence database and tools. The Physiochemical parameters like amino acid propensity, molecular weight, isoelectric point, aliphatic index, hydropathicity were determined. 28T he secondary structure of clgR was predicted using SOPMA secondary28T 28Tstructure method. The 3D structure was predicted using SWISS-MODEL server and model was further validated using PROCHECK analysis tool. The function of clgR was identified by Pfam domain database. |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://ijiset.com/vol5/v5s3/IJISET_V5_I03_01.pdf |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |