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In order for it to maintain its integrity, a cell relies on chaperonins (proteins) to correctly fold the long chains of bonded amino acids, called polypeptides. Chaperonins are essential for the folding and function of proteins in a wide number of cellular processes. Defective protein folding has been linked to a large number of human diseases such as cancer, heart disease, and Alzheimer’s and Huntingdon so understanding the role these chaperonins play could help to provide effective therapies.
TRiC chaperonin is essential for the folding and function of a growing list of proteins driving diverse cellular processes, including cytoskeletal proteins actin and tubulin. It can also suppress the misfolding and aggregation of neurotoxic proteins.
Previous studies have determined the structure of this chaperonin, but few have been able to fully understand what takes place within its interior chamber. In this study Pfizer use cryo-EM at Diamond to determine the interactions that take place during the folding process, and to understand the role of substrates in promoting the TRiC chaperonin’s function. In this study, The findings from this study could help scientists to build effective drugs to disrupt TRiC engagement with human disease.
Diamond Light Source is the UK's national synchrotron science facility, located at the Harwell Science and Innovation Campus in Oxfordshire.
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