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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Host-membrane interacting interface of the SARS coronavirus envelope protein: Immense functional potential of C-terminal domain
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Host-membrane interacting interface of the SARS coronavirus envelope protein: Immense functional potential of C-terminal domain

机译:Host-Membrane SARS Coronavirus包膜蛋白质的相互作用界面:C末端结构域的巨大功能势

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摘要

The Envelope (E) protein in SARS Coronavirus (CoV) is a small structural protein, incorporated as part of the envelope. A major fraction of the protein has been known to be associated with the host membranes, particularly organelles related to intracellular trafficking, prompting CoV packaging and propagation. Studies have elucidated the central hydrophobic transmembrane domain of the E protein being responsible for much of the viroporin activity in favor of the virus. However, newer insights into the organizational principles at the membranous compartments within the host cells suggest further complexity of the system. The lesser hydrophobic Carboxylic-terminal of the protein harbors interesting amino acid sequences- suggesting at the prevalence of membrane-directed amyloidogenic properties that remains mostly elusive. These highly conserved segments indicate at several potential membrane-associated functional roles that can redefine our comprehensive understanding of the protein. This should prompt further studies in designing and characterizing of effective targeted therapeutic measures.
机译:SARS冠状病毒(COV)中的封套(E)蛋白是一种小型结构蛋白,其作为包络的一部分。已知蛋白质的主要部分与宿主膜,特别是与细胞内运输相关的细胞器有关,提示COV包装和繁殖。研究阐明了E蛋白的中央疏水性跨膜结构域,该蛋白质负责疾病的大部分疾病活性有利于病毒。但是,宿主细胞内膜隔室的组织原则的新见解表明系统的进一步复杂性。蛋白质腹膜疏水羧酸末端的较小氨基酸序列 - 表明仍然难以捉摸的膜引导的淀粉样蛋白特性的患病率。这些高度保守的段表明了几种潜在的膜相关功能作用,可以重新定义我们对蛋白质的全面了解。这应该提示进一步研究设计和表征有效的有效的疗效。

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