Dnak SBD C-terminus E.Coli
Description
Product Specs
MDVKDVLLLD VTPLSLGIET MGGVMTTLIA KNTTIPTKHS QVFSTAEDNQ SAVTIHVLQGERKRAADNKS LGQFNLDGIN PAPRGMPQIE VTFDIDADGI LHVSAKDKNS GKEQKITIKA SSGLNEDEIQ KMVRDAEANA EADRKFEELV QTRNQGDHLL HSTRKQVEEA GDKLPADDKTAIESALTALE TALKGEDKAA IEAKMQELAQ VSQKLMEIAQ QQHAQQQTAG ADASANNAKD DDVVDAEFEE VKDKK.
Product Science Overview
The DnaK protein is a member of the Hsp70 family of heat shock proteins, which play a crucial role in the cellular response to stress by assisting in the proper folding of nascent polypeptides and the refolding of misfolded or aggregated proteins. The substrate binding domain (SBD) of DnaK is particularly important for its function, as it directly interacts with the polypeptide substrates. The C-terminal region of the SBD is essential for the binding and release of these substrates.
DnaK is composed of two main domains: the N-terminal nucleotide-binding domain (NBD) and the C-terminal substrate-binding domain (SBD). The SBD itself is further divided into two subdomains: the β-sandwich subdomain and the α-helical lid subdomain. The C-terminal region of the SBD, which includes the α-helical lid, is responsible for the regulation of substrate binding and release through conformational changes .
The interaction between the NBD and SBD is crucial for the allosteric regulation of DnaK’s activity. When ATP binds to the NBD, it induces a conformational change that opens the SBD, allowing substrate binding. Conversely, ATP hydrolysis and ADP release lead to the closing of the SBD, trapping the substrate .
The recombinant expression of the DnaK substrate binding domain C-terminal in Escherichia coli involves cloning the gene encoding this region into an expression vector. This allows for the production of large quantities of the protein for research and industrial applications. The protein coding region of the substrate binding domain of DnaK (amino acids 385-638) is typically amplified by polymerase chain reaction (PCR) and cloned into an E. coli expression vector .
The recombinant DnaK substrate binding domain C-terminal is used in various studies to understand the mechanisms of protein folding and the cellular response to stress. It is also employed in the development of therapeutic strategies for diseases caused by protein misfolding and aggregation, such as neurodegenerative disorders.
In addition, the study of DnaK and its interactions with substrates provides insights into the broader protein quality control (PQC) network in cells. This network includes other chaperones and proteases that work together to maintain protein homeostasis by refolding misfolded proteins, preventing their aggregation, or directing them for degradation .
