Substrate binding site flexibility of the small heat shock protein molecular chaperones

Substrate binding site flexibility of the small heat shock protein molecular chaperones.

Small heat shock proteins (sHSPs) serve as a first line of defense against stress-induced cell damage by binding and maintaining denaturing proteins in a folding-competent state. In contrast to the well-defined substrate binding regions of ATP-dependent chaperones, interactions between sHSPs and substrates are poorly understood. Defining substrate-binding sites of sHSPs is key to understanding ...

Interactions between small heat shock protein subunits and substrate in small heat shock protein-substrate complexes.

Small heat shock proteins (sHSPs) are dynamic oligomeric proteins that bind unfolding proteins and protect them from irreversible aggregation. This binding results in the formation of sHSP-substrate complexes from which substrate can later be refolded. Interactions between sHSP and substrate in sHSP-substrate complexes and the mechanism by which substrate is transferred to ATP-dependent chapero...

Molecular chaperones: Small heat shock proteins in the limelight

Small heat shock proteins have been the Cinderellas of the molecular chaperone world, but now the crystal structure of a small heat shock protein has been solved and mutation of two human homologues implicated in genetic disease. Intermediate filaments appear to be one of the key targets of their chaperone activity.

The Biology of HEAT SHOCK PROTEINS and MOLECULAR CHAPERONES

The production of molecular clones of Toxoplasma gondii-derived heat shock protein 70 kDa

Toxoplasmosis is a common and widespread infection in humans and many other species of warm–blooded animals. Toxoplasma gondii-derived heat shock protein 70 (Hsp70) may play an important role in the virulence of Toxoplasma gondii (T. gondii). In the present study, T. gondii Hsp70 was amplified by polymerase chain reaction (PCR) from the DNA of the T. gondiitachyzoite RH strain through the use o...