Folding and Stability of Ankyrin Repeats Control Biological Protein Function
Ankyrin repeat proteins are found in all three kingdoms of life. Fundamentally, these proteins are involved in protein-protein interaction in order to activate or suppress biological processes. The basic architecture of these proteins comprises repeating modules forming elongated structures. Due to...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2021-06-01
|
| Series: | Biomolecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2218-273X/11/6/840 |
| _version_ | 1797531293562437632 |
|---|---|
| author | Amit Kumar Jochen Balbach |
| author_facet | Amit Kumar Jochen Balbach |
| author_sort | Amit Kumar |
| collection | DOAJ |
| description | Ankyrin repeat proteins are found in all three kingdoms of life. Fundamentally, these proteins are involved in protein-protein interaction in order to activate or suppress biological processes. The basic architecture of these proteins comprises repeating modules forming elongated structures. Due to the lack of long-range interactions, a graded stability among the repeats is the generic properties of this protein family determining both protein folding and biological function. Protein folding intermediates were frequently found to be key for the biological functions of repeat proteins. In this review, we discuss most recent findings addressing this close relation for ankyrin repeat proteins including DARPins, Notch receptor ankyrin repeat domain, IκBα inhibitor of NFκB, and CDK inhibitor p19<sup>INK4d</sup>. The role of local folding and unfolding and gradual stability of individual repeats will be discussed during protein folding, protein-protein interactions, and post-translational modifications. The conformational changes of these repeats function as molecular switches for biological regulation, a versatile property for modern drug discovery. |
| first_indexed | 2024-03-10T10:40:47Z |
| format | Article |
| id | doaj.art-29e828ac9a764e948c824e901a586b1f |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T10:40:47Z |
| publishDate | 2021-06-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-29e828ac9a764e948c824e901a586b1f2023-11-21T22:55:03ZengMDPI AGBiomolecules2218-273X2021-06-0111684010.3390/biom11060840Folding and Stability of Ankyrin Repeats Control Biological Protein FunctionAmit Kumar0Jochen Balbach1Department of Life Sciences, Faculty of Natural Sciences, Imperial College of Science, Technology and Medicine London, South Kensington, London SW7 2BU, UKInstitute of Physics, Biophysics, Martin Luther University Halle–Wittenberg, 06120 Halle, GermanyAnkyrin repeat proteins are found in all three kingdoms of life. Fundamentally, these proteins are involved in protein-protein interaction in order to activate or suppress biological processes. The basic architecture of these proteins comprises repeating modules forming elongated structures. Due to the lack of long-range interactions, a graded stability among the repeats is the generic properties of this protein family determining both protein folding and biological function. Protein folding intermediates were frequently found to be key for the biological functions of repeat proteins. In this review, we discuss most recent findings addressing this close relation for ankyrin repeat proteins including DARPins, Notch receptor ankyrin repeat domain, IκBα inhibitor of NFκB, and CDK inhibitor p19<sup>INK4d</sup>. The role of local folding and unfolding and gradual stability of individual repeats will be discussed during protein folding, protein-protein interactions, and post-translational modifications. The conformational changes of these repeats function as molecular switches for biological regulation, a versatile property for modern drug discovery.https://www.mdpi.com/2218-273X/11/6/840ankyrin repeat proteinsprotein stabilityprotein foldinglocal unfoldingmolecular switchpartial unfolding |
| spellingShingle | Amit Kumar Jochen Balbach Folding and Stability of Ankyrin Repeats Control Biological Protein Function Biomolecules ankyrin repeat proteins protein stability protein folding local unfolding molecular switch partial unfolding |
| title | Folding and Stability of Ankyrin Repeats Control Biological Protein Function |
| title_full | Folding and Stability of Ankyrin Repeats Control Biological Protein Function |
| title_fullStr | Folding and Stability of Ankyrin Repeats Control Biological Protein Function |
| title_full_unstemmed | Folding and Stability of Ankyrin Repeats Control Biological Protein Function |
| title_short | Folding and Stability of Ankyrin Repeats Control Biological Protein Function |
| title_sort | folding and stability of ankyrin repeats control biological protein function |
| topic | ankyrin repeat proteins protein stability protein folding local unfolding molecular switch partial unfolding |
| url | https://www.mdpi.com/2218-273X/11/6/840 |
| work_keys_str_mv | AT amitkumar foldingandstabilityofankyrinrepeatscontrolbiologicalproteinfunction AT jochenbalbach foldingandstabilityofankyrinrepeatscontrolbiologicalproteinfunction |