Complete 1H, 13C and 15N assignments of a monomeric, biologically active apolipoprotein E carboxyl-terminal domain.
Complete 1H, 13C and 15N assignments of a monomeric, biologically active apolipoprotein E carboxyl-terminal domain.
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完成单体、生物活性载脂蛋白 E 羧基末端结构域的 1H、13C 和 15N 分配。
DOI：
10.1023/b:jnmr.0000032517.98560.39
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发表时间：
2004
影响因子：
2.7
通讯作者：
Wang,Jianjun
中科院分区：
文献类型：
--
作者：
Fan,Daping;Korando,LeslieA;Dothager,RobinS;Li,Qianqian;Wang,Jianjun
Human apolipoprotein E (apoE) is a 299-residue exchangeable apolipoprotein that plays important roles in lipid and lipoprotein metabolism, neurobiology and several other biological processes (Weisgraber, 1994; Mahley et al., 2000). ApoE contains two structural and functional domains, a 22-kDa N-terminal domain (residues 1–191) and a 10-kDa C-terminal domain (residues 216–299)(Wetterau et al., 1988). The N-terminal domain is the LDL receptor-binding domain and also contains the major heparin-binding sites. The X-ray crystal structure of this domain displays an up-and-down four-helix bundle in the lipid-free state (Wilson et al., 1991). The C-terminal domain is responsible for lipoprotein binding. Lipid-free apoE tends to form oligomers and the C-terminal domain causes this oligomerization. The aggregation property of the C-terminal domain presents a major difficulty for the structural determination of the apoE C-terminal domain and full-length apoE. Efforts in the structural determination of the C-terminal domain and full-length apoE yielded a diffraction-quality crystal of a 50-residue fragment of the C-terminal domain (Forstner et al., 1999). However, no detailed structural information is available for either the full-length apoE or its C-terminal domain to date. In order to carry out NMR structural determination of the lipid-free apoE C-terminal domain, we successfully prepared a monomeric apoE C-terminal domain. This monomeric apoE C-terminal domain spans residues 200–299 and is biologically active in
