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A History of Molecular Chaperone Structures in the Protein Data Bank
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 prot...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6940948/ https://www.ncbi.nlm.nih.gov/pubmed/31817979 http://dx.doi.org/10.3390/ijms20246195 |
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author | Bascos, Neil Andrew D. Landry, Samuel J. |
author_facet | Bascos, Neil Andrew D. Landry, Samuel J. |
author_sort | Bascos, Neil Andrew D. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6940948 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-69409482020-01-09 A History of Molecular Chaperone Structures in the Protein Data Bank Bascos, Neil Andrew D. Landry, Samuel J. Int J Mol Sci Review 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. MDPI 2019-12-08 /pmc/articles/PMC6940948/ /pubmed/31817979 http://dx.doi.org/10.3390/ijms20246195 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Bascos, Neil Andrew D. Landry, Samuel J. A History of Molecular Chaperone Structures in the Protein Data Bank |
title | A History of Molecular Chaperone Structures in the Protein Data Bank |
title_full | A History of Molecular Chaperone Structures in the Protein Data Bank |
title_fullStr | A History of Molecular Chaperone Structures in the Protein Data Bank |
title_full_unstemmed | A History of Molecular Chaperone Structures in the Protein Data Bank |
title_short | A History of Molecular Chaperone Structures in the Protein Data Bank |
title_sort | history of molecular chaperone structures in the protein data bank |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6940948/ https://www.ncbi.nlm.nih.gov/pubmed/31817979 http://dx.doi.org/10.3390/ijms20246195 |
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