Anti-groEL antibody

Target data

Together with its co-chaperonin GroES, plays an essential role in assisting protein folding (PubMed : 10532860, PubMed : 16751100, PubMed : 1676490, PubMed : 18418386, PubMed : 18987317, PubMed : 20603018, PubMed : 24816391, PubMed : 2573517, PubMed : 2897629, PubMed : 8104102, PubMed : 9285593). The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding, probably by preventing aggregation and by entropically destabilizing folding intermediates (PubMed : 16751100, PubMed : 18418386, PubMed : 18987317, PubMed : 20603018, PubMed : 24816391). Rapid binding of ATP, followed by slower binding of the non-native substrate protein and GroES to the cis open ring of GroEL initiates productive folding of the non-native protein inside a highly stable GroEL-ATP-GroES complex (PubMed : 19915138, PubMed : 22445172, PubMed : 9285585, PubMed : 9285593). Binding of ATP and GroES induces conformational changes that result in the release of the substrate protein into a nano-cage compartment, within the GroEL central cavity, for folding in isolation (PubMed : 16684774, PubMed : 22445172, PubMed : 8861908, PubMed : 9285585). To discharge GroES and substrate protein, ATP hydrolysis in the cis ring is required to form a GroEL-ADP-GroES complex with decreased stability (PubMed : 9285593). Finally, binding of ATP to the opposite trans ring of GroEL results in disassembly of the cis-ternary complex, which opens the cage and allows release of the folded protein (PubMed : 9285585, PubMed : 9285593). Proteins released in non-native form may be rapidly rebound by another GroEL complex until all of the initially bound polypeptide reaches native form (PubMed : 7867798, PubMed : 7915201). Can rescue kinetically trapped intermediates (PubMed : 20603018). GroEL shows ATPase activity (PubMed : 1676490, PubMed : 379350, PubMed : 9285593). ATP hydrolysis moves the reaction cycle forward but is not required for substrate folding (PubMed : 9285593).. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.. (Microbial infection) Essential for the assembly of several bacteriophages.