fotoloha.blogg.se - Chaperone synonym

SBD contains a groove with an affinity for neutral, hydrophobic amino acid residues. The β sheet subdomain consists of stranded β sheets with upward protruding loops, as a typical β barrel, which enclose the peptide backbone of the substrate.

Substrate binding domain – is composed of a 15 kDa β sheet subdomain and a 10 kDa helical subdomain.

The exchange of ATP and ADP leads to conformational changes in the other two domains. The NBD (nucleotide binding domain) consists of two lobes with a deep cleft between them, at the bottom of which nucleotide (ATP and ADP) binds.

N-terminal ATPase domain – binds ATP ( Adenosine triphosphate) and hydrolyzes it to ADP ( Adenosine diphosphate).

The Hsp70 proteins have three major functional domains: Hsp70, heat shock protein 70 kDa NBD, N‐terminal nucleotide‐binding domain SBD, substrate binding domain at C‐terminal. (c) Secondary structures of Hsp70 virtualized using VMD 1.9.1 software.

(b) the complete amino acid sequence of human Hsp70 (UniProtKB identifier: P0DMV8) as a major stress‐inducible member of the Hsp70 family. EEVD‐motif participates in binding to co‐chaperones and other HSPs.

The NBD contains the ATP/ADP pocket that binds and The SBD contains a substrate‐binding pocket that interacts with extended polypeptides as substrate, an α‐helical subdomain from the C‐terminal side of SBD forms a flexible lid. The Hsp70s consist of two high conserved functional domains including an NBD and a C‐terminal substrate‐binding domain (SBD), also an EEVD‐motif at C‐terminal.