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Open AccessReview

A History of Molecular Chaperone Structures in the Protein Data Bank

Protein Structure and Immunology Laboratory, National Institute of Molecular Biology and Biotechnology University of the Philippines Diliman, Quezon City 1101, Philippines
Department of Biochemistry and Molecular Biology, Tulane University School of Medicine, New Orleans, LA 70112, USA
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(24), 6195;
Received: 22 November 2019 / Revised: 4 December 2019 / Accepted: 4 December 2019 / Published: 8 December 2019
(This article belongs to the Special Issue Molecular Chaperones 2.0)
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 several classes of Hsps (Hsp60, Hsp70, Hsp90, and Hsp104). When possible, it discusses the complete structures for these proteins, and the types of molecular machines to which they have been assigned. The structures of domains and the associated functions are discussed in order to illustrate the rationale for the proposed unfoldase function. View Full-Text
Keywords: chaperones; protein structure; protein functions; PDB chaperones; protein structure; protein functions; PDB
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MDPI and ACS Style

Bascos, N.A.D.; Landry, S.J. A History of Molecular Chaperone Structures in the Protein Data Bank. Int. J. Mol. Sci. 2019, 20, 6195.

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