Phosphorylation of SAMHD1 Thr592 increases C-terminal domain dynamics, tetramer dissociation and ssDNA binding kinetics

SAM and HD domain containing deoxynucleoside triphosphate triphosphohydrolase 1 (SAMHD1) is driven into its activated tetramer form by binding of GTP activator and dNTP activators/substrates. In addition, the inactive monomeric and dimeric forms of the enzyme bind to single-stranded (ss) nucleic aci...

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Detalles Bibliográficos
Autores principales: Orris, Benjamin, Huynh, Kevin W, Ammirati, Mark, Han, Seungil, Bolaños, Ben, Carmody, Jason, Petroski, Matthew D, Bosbach, Benedikt, Shields, David J, Stivers, James T
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2022
Materias:
Nucleic Acid Enzymes
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9303311/
https://www.ncbi.nlm.nih.gov/pubmed/35801923
http://dx.doi.org/10.1093/nar/gkac573

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9303311/
https://www.ncbi.nlm.nih.gov/pubmed/35801923
http://dx.doi.org/10.1093/nar/gkac573

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