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首页> 外文期刊>Journal of Molecular Biology >Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein.
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Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein.

机译：肉豆蔻基化和非肉豆蔻基化的HIV-1 Nef蛋白的锚结构域的结构。

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摘要

Negative factor (Nef) is a regulatory myristoylated protein of human immunodeficiency virus (HIV) that has a two-domain structure consisting of an anchor domain and a core domain separated by a specific cleavage site of the HIV proteases. For structural analysis, the HIV-1 Nef anchor domain (residues 2-57) was synthesized with a myristoylated and non-myristoylated N terminus. The structures of the two peptides were studied by1H NMR spectroscopy and a structural model was obtained by restrained molecular dynamic simulations. The non-myristoylated peptide does not have a unique, compactly folded structure but occurs in a relatively extended conformation. The only rather well-defined canonical secondary structure element is a short two-turn alpha-helix (H2) between Arg35 and Gly41. A tendency for another helical secondary structure element (H1) can be observed for the arginine-rich region (Arg17 to Arg22). Myristoylation of the N-terminal glycine residue leads to stabilization of both helices, H1 and H2. The first helix in the arginine-rich region is stabilized by the myristoylation and now contains residues Pro14 to Arg22. The second helix appears to be better defined and to contain more residues (Ala33 to Gly41) than in the absence of myristoylation. In addition, the hydrophobic N-terminal myristic acid residue interacts closely with the side-chain of Trp5 and thereby forms a loop with Gly2, Gly3 and Lys4 in the kink region. This interaction could possibly be disturbed by phosphorylation of a nearby serine residue, and modifiy the characteristic membrane interactions of the HIV-1 Nef anchor domain. Copyright 1999 Academic Press.
机译：负因子（Nef）是人免疫缺陷病毒（HIV）的一种调节性肉豆蔻酰化蛋白，具有由锚定结构域和核心结构域组成的两个结构域结构，该结构域由HIV蛋白酶的特定切割位点隔开。为了进行结构分析，将HIV-1 Nef锚结构域（残基2-57）与一个肉豆蔻酰化的和非肉豆蔻酰化的N末端合成。通过1 H NMR光谱研究了这两种肽的结构，并通过限制性分子动力学模拟获得了结构模型。非肉豆蔻酰化的肽不具有独特的紧密折叠的结构，而是以相对延伸的构象出现。唯一定义明确的规范二级结构元素是Arg35和Gly41之间的短两匝α-螺旋（H2）。对于富含精氨酸的区域（Arg17至Arg22），可以观察到另一种螺旋二级结构元素（H1）的趋势。 N末端甘氨酸残基的肉豆蔻酰基化导致两个螺旋H1和H2的稳定。富含精氨酸的区域中的第一个螺旋通过肉豆蔻酰化作用得以稳定，现在包含残基Pro14至Arg22。与没有肉豆蔻酰化的情况相比，第二个螺旋的定义似乎更好，并且包含更多的残基（Ala33至Gly41）。另外，疏水性N-末端肉豆蔻酸残基与Trp5的侧链紧密相互作用，从而在扭结区域中与Gly2，Gly3和Lys4形成环。这种相互作用可能被附近丝氨酸残基的磷酸化所干扰，并修饰了HIV-1 Nef锚定域的特征性膜相互作用。版权所有1999，学术出版社。

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