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- W2955202122 abstract "Nucleic acid editing enzymes are essential components of the human immune system that lethally mutate viral pathogens and somatically mutate immunoglobulins. Among these enzymes are cytidine deaminases of the apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like (APOBEC) super family, each with unique target sequence specificity and subcellular localization. We focus on the DNA-editing APOBEC3 enzymes that have recently attracted attention because of their involvement in cancer and potential in gene-editing applications. We review and compare the crystal structures of APOBEC3 (A3) domains, binding interactions with DNA, substrate specificity, and activity. Recent crystal structures of A3A and A3G bound to ssDNA have provided insights into substrate binding and specificity determinants of these enzymes. Still many unknowns remain regarding potential cooperativity, nucleic acid interactions, and systematic quantification of substrate preference of many APOBEC3s, which are needed to better characterize the biological functions and consequences of misregulation of these gene editors." @default.
- W2955202122 created "2019-07-12" @default.
- W2955202122 creator A5009290437 @default.
- W2955202122 creator A5068974276 @default.
- W2955202122 date "2019-07-10" @default.
- W2955202122 modified "2023-10-11" @default.
- W2955202122 title "APOBEC3s: DNA‐editing human cytidine deaminases" @default.
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- W2955202122 doi "https://doi.org/10.1002/pro.3670" @default.
- W2955202122 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6699113" @default.
- W2955202122 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31241202" @default.
- W2955202122 hasPublicationYear "2019" @default.
- W2955202122 type Work @default.
- W2955202122 sameAs 2955202122 @default.