Basic Science Program, Frederick National Laboratory for Cancer Research, Frederick, MD, 21702, USA.
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA, 01655, USA.
Curr Opin Struct Biol. 2021 Apr;67:195-204. doi: 10.1016/j.sbi.2020.12.004. Epub 2021 Jan 22.
APOBEC3 enzymes are key enzymes in our innate immune system regulating antiviral response in HIV and unfortunately adding diversity in cancer as they deaminate cytosine. Seven unique single and double domain APOBEC3s provide them with unique activity and specificity profiles for this deamination. Recent crystal and NMR structures of APOBEC3 complexes are unraveling the variety of epitopes involved in binding nucleic acids, including at the catalytic site, elsewhere on the catalytic domain and in the inactive N-terminal domain. The interplay between these diverse interactions is critical to uncovering the mechanisms by which APOBEC3s recognize and process their substrates.
APOBEC3 酶是我们先天免疫系统中的关键酶，调节 HIV 中的抗病毒反应，不幸的是，它们在癌症中使胞嘧啶脱氨酶化，增加了多样性。七种独特的单域和双域 APOBEC3 为其提供了独特的活性和特异性，用于这种脱氨反应。APOBEC3 复合物的最新晶体和 NMR 结构揭示了参与结合核酸的多种表位，包括在催化位点、催化结构域的其他部位和无活性的 N 端结构域。这些不同相互作用之间的相互作用对于揭示 APOBEC3 识别和处理其底物的机制至关重要。
