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首页> 外文期刊>Biochemistry >Structures and micelle locations of the nonlipidated and lipidated C-terminal membrane anchor of 2',3'-cyclic nucleotide-3'-phosphodiesterase
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Structures and micelle locations of the nonlipidated and lipidated C-terminal membrane anchor of 2',3'-cyclic nucleotide-3'-phosphodiesterase

机译：非玻璃化和脂质的C末端膜锚的结构和胶束位置为2'，3'-环状核苷酸-3'-磷酸二酯酶

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2,3'-Cyclic nucleotide-3'-phosphodiesterase (CNP) is a myelin-associated protein, an enzyme abundantly present in the central nervous system of mammals and some vertebrates. In vitro, CNP specifically catalyzes the hydrolysis of 2',3'-cyclic nucleotides to produce 2'-nucleotides, but the physiologically relevant in vivo substrate is still unknown. Recently, it was found that CNP is a possible linker protein between microtubules and the plasma membranes. Since CNP is modified post-translationally by an isoprenylation process at its C terminus, the prenylation is hypothesized to be a requisite process, which permanently anchors CNP to the plasma membrane. This study investigates the molecular mechanism of the interaction between CNP and the plasma membrane, proposing a general model to interpret the structural bases of prenylated proteins binding to the membrane. A 13 residue, C-terminal CNP fragment, C13, was demonstrated to be directly responsible for CNP membrane anchoring. C13 and its lipidated derivative (LIPO-C13) were subjected to conformational analysis in membrane mimetic environments, by means of CD and NMR spectroscopies. The orientation of C13 in relation to the membrane was investigated by NMR and EPR spin labeling studies, Our structural investigation shows that the presence of the lipidic tail is essential for the peptide to be folded and correctly positioned on the membrane surface. A general model is proposed in which the post-translational lipidation is an important biomolecular trick to enlarge the hydrophobic surface and to enable the contact of the protein with membrane.
机译：2,3'-循环核苷酸-3'-磷酸二酯酶（CNP）是一种髓鞘相关蛋白，一种在哺乳动物的中枢神经系统中大规模存在的酶和一些脊椎动物。体外，CNP特异性地催化2'，3'-环状核苷酸的水解，以产生2'-核苷酸，但体内底物的生理学相关仍然未知。最近，发现CNP是微管和血浆膜之间可能的接头蛋白。由于CNP通过其C末端的异戊二烯化方法翻译，因此将戊化物假设为必要的方法，该过程永久地将CNP锚固到质膜。本研究研究了CNP与质膜之间的相互作用的分子机制，提出了一种普通模型，解释戊酰化蛋白质与膜结合的普苯胺化蛋白的结构碱。证据证明了13个残基，C末端CNP片段C13直接负责CNP膜锚定。通过CD和NMR光谱对C13及其脂质化衍生物（Lipo-C13）进行膜模拟环境的构象分析。通过NMR和EPR旋转标记研究研究了C13关于膜的取向，我们的结构研究表明，脂质尾的存在对于肽折叠并正确定位在膜表面上是必需的。提出了一种通用模型，其中翻译后脂质是扩大疏水表面并使蛋白质与膜接触的重要生物分子技巧。

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