Scholarly open access journals, Peer-reviewed, and Refereed Journals, Impact factor 8.14 (Calculate by google scholar and Semantic Scholar | AI-Powered Research Tool) , Multidisciplinary, Monthly, Indexing in all major database & Metadata, Citation Generator, Digital Object Identifier(DOI)
The biological functions of proteins are governed by their proper folding and assembly. Protein chaperones are essential in all domains of life to prevent and resolve protein misfolding during translation and proteotoxic stress. Mycobacterium tuberculosis capsular heat shock protein DanK is a molecular chaperone. This chaperone interacts with protein substrates in an ATP-dependent manner to prevent aggregation and promote protein folding. This activity is stimulated by DnaJ and GrpE. ATP-dependent Mycobacterium DnaK (Hsp70) chaperone’s function is controlled in part by the nucleotide exchange factor (NEF) co-chaperone GrpE. Recently crystal structure of Mycobacterium tuberculosis DnaK has been deciphered but there is no three-dimensional structure of the DnaK-DnaJ and DnaK-GrpE complex reported to date. In this piece of work, we modeled the DnaJ and GrpE protein and docked with the crystal structures with DnaK.
Keywords:
DnaK, GrpE, DnaJ, GrpE, Chaperone, Hsp70
Cite Article:
"Interface analysis of DnaK-GrpE-DnaJ chaperon system of Mycobacterium tuberculosis", International Journal of Science & Engineering Development Research (www.ijrti.org), ISSN:2455-2631, Vol.7, Issue 7, page no.1470 - 1482, June-2022, Available :http://www.ijrti.org/papers/IJRTI2207231.pdf
Downloads:
000204897
ISSN:
2456-3315 | IMPACT FACTOR: 8.14 Calculated By Google Scholar| ESTD YEAR: 2016
An International Scholarly Open Access Journal, Peer-Reviewed, Refereed Journal Impact Factor 8.14 Calculate by Google Scholar and Semantic Scholar | AI-Powered Research Tool, Multidisciplinary, Monthly, Multilanguage Journal Indexing in All Major Database & Metadata, Citation Generator