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Structural insights into kinetoplastid coronin oligomerization domain and F-actin interaction
The two-domain actin associated protein coronin interacts with filamentous (F-) actin, facilitating diverse biological processes including cell proliferation, motility, phagocytosis, host-parasite interaction and cargo binding. The conserved N-terminal β-propeller domain is involved in protein: prot...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8554105/ https://www.ncbi.nlm.nih.gov/pubmed/34746809 http://dx.doi.org/10.1016/j.crstbi.2021.10.002 |
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author | Parihar, Pankaj Singh Singh, Aastha Karade, Sharanbasappa Shrimant Sahasrabuddhe, Amogh Anant Pratap, J. Venkatesh |
author_facet | Parihar, Pankaj Singh Singh, Aastha Karade, Sharanbasappa Shrimant Sahasrabuddhe, Amogh Anant Pratap, J. Venkatesh |
author_sort | Parihar, Pankaj Singh |
collection | PubMed |
description | The two-domain actin associated protein coronin interacts with filamentous (F-) actin, facilitating diverse biological processes including cell proliferation, motility, phagocytosis, host-parasite interaction and cargo binding. The conserved N-terminal β-propeller domain is involved in protein: protein interactions, while the C-terminal coiled-coil domain mediates oligomerization, transducing conformational changes. The L. donovani coronin coiled-coil (LdCoroCC) domain exhibited a novel topology and oligomer association with an inherent asymmetry, caused primarily by three a residues of successive heptads. In the T.brucei homolog (TbrCoro), two of these ‘a’ residues are different (Val 493 & 507 replacing LdCoroCC Ile 486 and Met 500 respectively). The elucidated structure possesses a similar topology and assembly while comparative structural analysis shows that the T.brucei coronin coiled-coil domain (TbrCoroCC) too possesses the asymmetry though its magnitude is smaller. Analysis identifies that the asymmetric state is stabilized via cyclic salt bridges formed by Arg 497 and Glu 504. Co-localization studies (LdCoro, TbrCoro and corresponding mutant coiled coil constructs) with actin show that there are subtle differences in their binding patterns, with the double mutant V493I–V507M showing maximal effect. None of the constructs have an effect on F-actin length. Taken together with LdCoroCC, we therefore conclude that the inherent asymmetric structures are essential for kinetoplastids, and are of interest in understanding and exploiting actin dynamics. |
format | Online Article Text |
id | pubmed-8554105 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-85541052021-11-04 Structural insights into kinetoplastid coronin oligomerization domain and F-actin interaction Parihar, Pankaj Singh Singh, Aastha Karade, Sharanbasappa Shrimant Sahasrabuddhe, Amogh Anant Pratap, J. Venkatesh Curr Res Struct Biol Research Article The two-domain actin associated protein coronin interacts with filamentous (F-) actin, facilitating diverse biological processes including cell proliferation, motility, phagocytosis, host-parasite interaction and cargo binding. The conserved N-terminal β-propeller domain is involved in protein: protein interactions, while the C-terminal coiled-coil domain mediates oligomerization, transducing conformational changes. The L. donovani coronin coiled-coil (LdCoroCC) domain exhibited a novel topology and oligomer association with an inherent asymmetry, caused primarily by three a residues of successive heptads. In the T.brucei homolog (TbrCoro), two of these ‘a’ residues are different (Val 493 & 507 replacing LdCoroCC Ile 486 and Met 500 respectively). The elucidated structure possesses a similar topology and assembly while comparative structural analysis shows that the T.brucei coronin coiled-coil domain (TbrCoroCC) too possesses the asymmetry though its magnitude is smaller. Analysis identifies that the asymmetric state is stabilized via cyclic salt bridges formed by Arg 497 and Glu 504. Co-localization studies (LdCoro, TbrCoro and corresponding mutant coiled coil constructs) with actin show that there are subtle differences in their binding patterns, with the double mutant V493I–V507M showing maximal effect. None of the constructs have an effect on F-actin length. Taken together with LdCoroCC, we therefore conclude that the inherent asymmetric structures are essential for kinetoplastids, and are of interest in understanding and exploiting actin dynamics. Elsevier 2021-10-14 /pmc/articles/PMC8554105/ /pubmed/34746809 http://dx.doi.org/10.1016/j.crstbi.2021.10.002 Text en © 2021 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Research Article Parihar, Pankaj Singh Singh, Aastha Karade, Sharanbasappa Shrimant Sahasrabuddhe, Amogh Anant Pratap, J. Venkatesh Structural insights into kinetoplastid coronin oligomerization domain and F-actin interaction |
title | Structural insights into kinetoplastid coronin oligomerization domain and F-actin interaction |
title_full | Structural insights into kinetoplastid coronin oligomerization domain and F-actin interaction |
title_fullStr | Structural insights into kinetoplastid coronin oligomerization domain and F-actin interaction |
title_full_unstemmed | Structural insights into kinetoplastid coronin oligomerization domain and F-actin interaction |
title_short | Structural insights into kinetoplastid coronin oligomerization domain and F-actin interaction |
title_sort | structural insights into kinetoplastid coronin oligomerization domain and f-actin interaction |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8554105/ https://www.ncbi.nlm.nih.gov/pubmed/34746809 http://dx.doi.org/10.1016/j.crstbi.2021.10.002 |
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