NMR assignments and the identification of the secondary structure of the anti-retroviral cytidine deaminase.
NMR assignments and the identification of the secondary structure of the anti-retroviral cytidine deaminase.
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DOI：
10.1093/nass/nrn093
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发表时间：
2008-01-01
期刊：
影响因子：
--
通讯作者：
Katahira, Masato
中科院分区：
文献类型：
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作者：
Furukawa, Ayako;Nagata, Takashi;Katahira, Masato
APOBEC3G(载脂蛋白B信使核糖核酸编辑酶催化多肽样3G)被认为在针对人类免疫缺陷病毒1型(HIV-1)的固有细胞免疫中发挥作用。APOBEC3G(APO3G)的抗逆转录病毒活性与病毒DNA通过胞苷脱氨基发生超突变有关。APO3G含有两个胞苷脱氨酶结构域，其特征是高度保守的锌配位基序。目前已知只有APO3G的C-末端结构域(c-APO3G)具有催化活性。为了阐明APO3G灭活HIV-1的分子机制，我们进行了结构和结合的核磁共振研究。在这里，我们展示了c-APO3G主链归属的结果，以及根据化学位移指数(CSI)和NOE数据推断的二级结构的识别。
APOBEC3G (apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3G) is known to have a role in intrinsic cellular immunity against human immunodeficiency virus type1 (HIV-1). The antiretroviral activity of APOBEC3G (APO3G) is associated with the hypermutation of viral DNA through cytidine deamination. APO3G contains two cytidine deaminase domains that are characterised by highly conserved zinc-coordinating motif. It is known that only the C-terminal domain of APO3G (c-APO3G) has the catalytic activity. To shed light on the molecular mechanism of action by which APO3G inactivates HIV-1, we have undertaken the structural and binding studies by NMR. Here, we show the achievement of backbone assignments of c-APO3G and the identification of the secondary structure deduced from chemical shift index (CSI) and NOE data.