人载脂蛋白 E 两种异构体的 N 端结构域的 H、N 和 C 化学位移赋值。
H, N and C chemical shift assignments of the N-terminal domain of the two isoforms of the human apolipoprotein E.
机构信息
Tata Institute of Fundamental Research, 36/P, Gopanpally Village, Serilingampally Mandal, Ranga Reddy District, 500107, Hyderabad, India.
出版信息
Biomol NMR Assign. 2022 Oct;16(2):191-196. doi: 10.1007/s12104-022-10078-3. Epub 2022 Apr 22.
Apolipoprotein E (ApoE) is one of the major lipid transporters in humans. It is also implicated in pathological conditions like Alzheimer's and cardiovascular diseases. The N-terminal domain of ApoE binds low-density lipoprotein receptors (LDLR) while the C-terminal domain binds to the lipid. I report the backbone and aliphatic side-chain NMR chemical shifts of the N-terminal domain of two isoforms of ApoE, namely ApoE3 NTD (BMRB No. 51,122) and ApoE4 NTD (BMRB No. 51,123) at pH 3.5 (20 °C).
载脂蛋白 E（ApoE）是人类主要的脂质转运蛋白之一。它也与阿尔茨海默病和心血管疾病等病理状况有关。ApoE 的 N 端结构域与低密度脂蛋白受体（LDLR）结合，而 C 端结构域与脂质结合。我报告了两种 ApoE 异构体的 N 端结构域的骨架和脂肪侧链 NMR 化学位移，即 ApoE3 NTD（BMRB No.51,122）和 ApoE4 NTD（BMRB No.51,123），在 pH3.5（20°C）下。
Zotero 插件