Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification
SAMHD1 catalyses the dephosphorylation of deoxynucleotide triphosphates (dNTPs) and has antiretroviral activity. Here, the authors present the crystal structures of SAMHD1-oligonucleotide complexes, which reveal that the allosteric binding sites of SAMHD1 are plastic and can fit oligonucleotides in...
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Nature Portfolio
2021
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oai:doaj.org-article:235030ae21f844b790931e36a84dca122021-12-02T10:44:12ZNucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification10.1038/s41467-021-21023-82041-1723https://doaj.org/article/235030ae21f844b790931e36a84dca122021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21023-8https://doaj.org/toc/2041-1723SAMHD1 catalyses the dephosphorylation of deoxynucleotide triphosphates (dNTPs) and has antiretroviral activity. Here, the authors present the crystal structures of SAMHD1-oligonucleotide complexes, which reveal that the allosteric binding sites of SAMHD1 are plastic and can fit oligonucleotides in place of the two allosteric activators GTP and dNTP, and they also show that SAMHD1 recognises GpsN phosphorothioation modifications in nucleic acids, which is of interest in drug design.Corey H. YuAkash BhattacharyaMirjana PersaudAlexander B. TaylorZhonghua WangAngel Bulnes-RamosJoella XuAnastasia SelyutinaAlicia Martinez-LopezKristin CanoBorries DemelerBaek KimStephen C. HardiesFelipe Diaz-GrifferoDmitri N. IvanovNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021) |
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Science Q Corey H. Yu Akash Bhattacharya Mirjana Persaud Alexander B. Taylor Zhonghua Wang Angel Bulnes-Ramos Joella Xu Anastasia Selyutina Alicia Martinez-Lopez Kristin Cano Borries Demeler Baek Kim Stephen C. Hardies Felipe Diaz-Griffero Dmitri N. Ivanov Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification |
description |
SAMHD1 catalyses the dephosphorylation of deoxynucleotide triphosphates (dNTPs) and has antiretroviral activity. Here, the authors present the crystal structures of SAMHD1-oligonucleotide complexes, which reveal that the allosteric binding sites of SAMHD1 are plastic and can fit oligonucleotides in place of the two allosteric activators GTP and dNTP, and they also show that SAMHD1 recognises GpsN phosphorothioation modifications in nucleic acids, which is of interest in drug design. |
format |
article |
author |
Corey H. Yu Akash Bhattacharya Mirjana Persaud Alexander B. Taylor Zhonghua Wang Angel Bulnes-Ramos Joella Xu Anastasia Selyutina Alicia Martinez-Lopez Kristin Cano Borries Demeler Baek Kim Stephen C. Hardies Felipe Diaz-Griffero Dmitri N. Ivanov |
author_facet |
Corey H. Yu Akash Bhattacharya Mirjana Persaud Alexander B. Taylor Zhonghua Wang Angel Bulnes-Ramos Joella Xu Anastasia Selyutina Alicia Martinez-Lopez Kristin Cano Borries Demeler Baek Kim Stephen C. Hardies Felipe Diaz-Griffero Dmitri N. Ivanov |
author_sort |
Corey H. Yu |
title |
Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification |
title_short |
Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification |
title_full |
Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification |
title_fullStr |
Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification |
title_full_unstemmed |
Nucleic acid binding by SAMHD1 contributes to the antiretroviral activity and is enhanced by the GpsN modification |
title_sort |
nucleic acid binding by samhd1 contributes to the antiretroviral activity and is enhanced by the gpsn modification |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/235030ae21f844b790931e36a84dca12 |
work_keys_str_mv |
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