NMR structural studies of the myristoylated N-terminus of ADP ribosylation factor 6 (Arf6)
NMR structural studies of the myristoylated N-terminus of ADP ribosylation factor 6 (Arf6)
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DOI：
10.1016/j.febslet.2006.06.086
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发表时间：
2006-07-24
期刊：
影响因子：
3.5
通讯作者：
Oswald, Robert
中科院分区：
文献类型：
--
作者：
Gizachew, Dawit;Oswald, Robert
ARF蛋白是一种鸟嘌呤核苷酸结合蛋白，与内吞途径和囊泡运输有关。Arf蛋白的两种亚型(Arf1和Arf6)具有不同的细胞功能和定位，但结构相似。ARF蛋白有一个带有共价结合肉豆蔻基的N-末端螺旋。除了结构模型外，没有肉豆蔻酰化的N-端肽或完整的肉豆蔻酰化Arf蛋白的三维结构。然而，根据其分子结构的细节来理解肉豆蔻基和N-白蚁螺旋的作用是非常有意义的。在本文所述的Arf6的肉豆蔻酰化N-末端多肽的溶液结构中，肉豆蔻基向N-末端折叠，以与疏水残基特别是苯环相互作用。此外，十二烷基磷胆碱(DPC)胶束的结构和顺磁学研究表明，肉豆蔻基插入胶束中，而V4-G10残基与胶束表面相互作用。Arf6的非结合和胶束结合的肉豆蔻酰化N端肽的结构差异涉及肉豆蔻基和疏水残基的侧链。(C)2006年欧洲生化学会联合会。爱思唯尔出版，版权所有。
Arf proteins are guanine nucleotide binding proteins that are implicated in endocytotic pathways and vesicle trafficking. The two widely studied isoforms of Arf proteins (Arf1 and Arf6) have different cellular functions and localizations but similar structures. Arf proteins have an N-terminal helix with a covalently bound myristoyl group. Except structural models, there are no three dimensional structures of the myristoylated N-terminal peptide or the intact myristoylated Arf proteins. However, understanding the role of both the myristoyl group and the N-termitial helix based on the details of their molecular structures is of great interest. In the solution structure of myristoylated N-terminal peptide of Arf6 described here, the myristoyl group folds toward the N-terminus to interact with the hydrophobic residues in particular, the phenyl ring. Also, the structure of the dodecylphosphocholine (DPC) micelle-bound of the peptide together with paramagnetic studies showed that the myristoyl group is inserted into the micelle while residues V4-G10 interact with the surface of the micelle. The structural differences between the unbound and micelle-bound myristoylated N-terminal peptide of Arf6 involves the myristoyl group and the side chains of the hydrophobic residues. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.