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首页> 外文期刊>Biochemistry >Stability and Membrane Orientation of the Fukutin Transmembrane Domain: A Combined Multiscale Molecular Dynamics and Circular Dichroism Study
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Stability and Membrane Orientation of the Fukutin Transmembrane Domain: A Combined Multiscale Molecular Dynamics and Circular Dichroism Study

机译：福田跨膜域的稳定性和膜取向：结合多尺度分子动力学和圆二色性研究。

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The N-terminal domain of fukutin-I has been implicated in the localization of the protein in thenendoplasmic reticulumandGolgiApparatus. It has been proposed tomediate this through its interaction withnthe thinner lipid bilayers found in these compartments. Here we have employed multiscale molecular dy-nnamics simulations and circular dichroismspectroscopy to explore the structure, stability, and orientation of thenshort 36-residue N-terminus of fukutin-I (FK1TMD) in lipids with differing tail lengths. Our results show thatnFK1TMD adopts a stable helical conformation in phosphatidylcholine lipids when oriented with its principalnaxis perpendicular to the bilayer plane. The stability of the helix is largely insensitive to the lipid tail length,npreventing hydrophobic mismatch by virtue of its mobility and ability to tilt within the lipid bilayers. Thisnsuggests that changes in FK1TMDtilt in response to bilayer propertiesmay be implicated in the regulation of itsntrafficking. Coarse-grained simulations of the complex Golgi membrane suggest the N-terminal domain mayninduce the formation of microdomains in the surrounding membrane through its preferential interaction withn1,2-dipalmitoyl-sn-glycero-3-phosphatidylinositol 4,5-bisphosphate lipids.
机译：福建汀-I的N-末端结构域已被认为与蛋白质在内质网状高尔基体中的定位有关。已经提议通过其与在这些隔室中发现的较薄的脂质双层相互作用来介导该作用。在这里，我们采用了多尺度分子动力学模拟和圆二色光谱技术，以研究尾巴长度不同的脂质中福建汀-I短的36个残基N端（FK1TMD）的结构，稳定性和取向。我们的结果表明，nFK1TMD的磷脂酰胆碱脂类的主轴线垂直于双层平面取向时，它在磷脂酰胆碱脂质中采用稳定的螺旋构象。螺旋的稳定性对脂质尾巴的长度非常不敏感，由于其迁移率和在脂质双层中的倾斜能力，可以防止疏水性错配。这表明FK1TMDtilt响应双层特性的变化可能与其贩运的调控有关。复杂的高尔基体膜的粗粒度模拟表明，N末端结构域可通过其与n1,2-二棕榈酰-sn-甘油-3-磷脂酰肌醇4,5-双磷酸脂的优先相互作用而诱导周围膜中微区的形成。

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