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(1)H, (15)N and (13)C resonance assignments of the HR1c domain of PRK1, a protein kinase C-related kinase
PRK1 is a member of the protein kinase C-related kinase (PRK) family of serine/threonine kinases and a downstream effector of Rho GTPases. PRK1 has three N-terminal Homology Region 1 (HR1) domains (HR1a, HR1b and HR1c), which form antiparallel coiled coils that interact with Rho family GTPases. PRK1...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Springer Netherlands
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7462907/ https://www.ncbi.nlm.nih.gov/pubmed/32500230 http://dx.doi.org/10.1007/s12104-020-09954-7 |
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author | Sophocleous, Georgios Wood, George Owen, Darerca Mott, Helen R. |
author_facet | Sophocleous, Georgios Wood, George Owen, Darerca Mott, Helen R. |
author_sort | Sophocleous, Georgios |
collection | PubMed |
description | PRK1 is a member of the protein kinase C-related kinase (PRK) family of serine/threonine kinases and a downstream effector of Rho GTPases. PRK1 has three N-terminal Homology Region 1 (HR1) domains (HR1a, HR1b and HR1c), which form antiparallel coiled coils that interact with Rho family GTPases. PRK1 also has a C2-like domain that targets it to the plasma membrane and a kinase domain, which is a member of the protein kinase C superfamily. PRK1 is involved in cytoskeletal regulation, cell adhesion, cell cycle progression and the immune response, and is implicated in cancer. There is currently no structural information for the HR1c domain. The (1)H, (15)N and (13)C NMR backbone and sidechain resonance assignment of the HR1c domain presented here forms the basis for this domain’s structural characterisation. This work will also enable studies of interactions between the three HR1 domains in an effort to obtain structural insight into the regulation of PRK1 activity. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s12104-020-09954-7) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-7462907 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-74629072020-09-11 (1)H, (15)N and (13)C resonance assignments of the HR1c domain of PRK1, a protein kinase C-related kinase Sophocleous, Georgios Wood, George Owen, Darerca Mott, Helen R. Biomol NMR Assign Article PRK1 is a member of the protein kinase C-related kinase (PRK) family of serine/threonine kinases and a downstream effector of Rho GTPases. PRK1 has three N-terminal Homology Region 1 (HR1) domains (HR1a, HR1b and HR1c), which form antiparallel coiled coils that interact with Rho family GTPases. PRK1 also has a C2-like domain that targets it to the plasma membrane and a kinase domain, which is a member of the protein kinase C superfamily. PRK1 is involved in cytoskeletal regulation, cell adhesion, cell cycle progression and the immune response, and is implicated in cancer. There is currently no structural information for the HR1c domain. The (1)H, (15)N and (13)C NMR backbone and sidechain resonance assignment of the HR1c domain presented here forms the basis for this domain’s structural characterisation. This work will also enable studies of interactions between the three HR1 domains in an effort to obtain structural insight into the regulation of PRK1 activity. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s12104-020-09954-7) contains supplementary material, which is available to authorized users. Springer Netherlands 2020-06-04 2020 /pmc/articles/PMC7462907/ /pubmed/32500230 http://dx.doi.org/10.1007/s12104-020-09954-7 Text en © The Author(s) 2020 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Sophocleous, Georgios Wood, George Owen, Darerca Mott, Helen R. (1)H, (15)N and (13)C resonance assignments of the HR1c domain of PRK1, a protein kinase C-related kinase |
title | (1)H, (15)N and (13)C resonance assignments of the HR1c domain of PRK1, a protein kinase C-related kinase |
title_full | (1)H, (15)N and (13)C resonance assignments of the HR1c domain of PRK1, a protein kinase C-related kinase |
title_fullStr | (1)H, (15)N and (13)C resonance assignments of the HR1c domain of PRK1, a protein kinase C-related kinase |
title_full_unstemmed | (1)H, (15)N and (13)C resonance assignments of the HR1c domain of PRK1, a protein kinase C-related kinase |
title_short | (1)H, (15)N and (13)C resonance assignments of the HR1c domain of PRK1, a protein kinase C-related kinase |
title_sort | (1)h, (15)n and (13)c resonance assignments of the hr1c domain of prk1, a protein kinase c-related kinase |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7462907/ https://www.ncbi.nlm.nih.gov/pubmed/32500230 http://dx.doi.org/10.1007/s12104-020-09954-7 |
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