A History of Molecular Chaperone Structures in the Protein Data Bank.

ABSTRACT: Thirty years ago a class of proteins was found to prevent the aggregation of Rubisco. These proteins' ability to prevent unwanted associations led to their being called chaperones. These chaperone proteins also increased in expression as a response to heat shock, hence their label as heat shock proteins (Hsps). However, neither label encompasses the breadth of these proteins' functional capabilities. The term "unfoldases" has been proposed, as this basic function is shared by most members of this protein family. Onto this is added specializations that allow the different family members to perform various cellular functions. This current article focuses on the resolved structural bases for these functions. It reviews the currently available molecular structures in the Protein Data Bank for

SUBMITTER: Bascos NAD 

PROVIDER: S-EPMC6940948 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature