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Study of the protein structure analysis and molecular evolution of E-selectin in Homo sapiens

机译:智人E-选择蛋白的蛋白质结构分析与分子进化研究

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E-selectin is a cell adhesion molecule expressed only on endothelial cells activated by cytokines. During inflammation, E-selectin plays an important role in recruiting leukocytes to the site of injury. In humans, E-selectin is encoded by the SELE gene. To better understand the expression and regulation of E-selectin gene, we analyzed the protein structure of E-selectin in human and molecular evolution of its gene in 9 vertebrate animals with bioinformatic softwares and network resources. Results showed that E-selectin is an unstable hydrophilic membrane protein with only one transmembrane domain as well as a signal peptide. The secondary structure is composed of α-helix (11.31%), extended strand (25.74%), and random coil (62.95%). The molecular evolution analysis revealed that the 9 vertebrates were divided into two major branches, one of which includes Bos Taurus, Ovis aries, Odocoileus hemionus, Sus scrofa, Canis Iupus familiaris, Equus caballus and the other is for Homo sapiens, Mus musculus, and Rattus norvegicus. This phylogenetic tree was consistent well with recognized evolutionary relationship among these species. In this research, we investigated the basic protein structure and molecular evolution of E-selectin in Homo sapiens, which will help us to understand how diseases and infection can be controlled in molecular level, and to develop specific drugs based on this knowledge.
机译:E-选择蛋白是仅在被细胞因子激活的内皮细胞上表达的细胞粘附分子。在发炎期间,E-选择素在将白细胞募集到损伤部位中起重要作用。在人类中,E-选择蛋白由SELE基因编码。为了更好地了解E-选择素基因的表达和调控,我们利用生物信息学软件和网络资源分析了9种脊椎动物中人E-选择素的蛋白质结构及其基因的分子进化。结果表明,E-选择蛋白是一种不稳定的亲水膜蛋白,仅具有一个跨膜结构域以及一个信号肽。二级结构由α-螺旋(11.31%),延伸链(25.74%)和无规卷曲(62.95%)组成。分子进化分析显示,这9个脊椎动物被分为两个主要分支,其中一个包括Bos Taurus,Ovis aries,Odocoileus hemionus,Sus scrofa,Canis Iupus熟悉,Equus caballus,另一个则属于智人,Mus musculus和褐家鼠这种系统发育树与这些物种之间公认的进化关系非常吻合。在这项研究中,我们研究了智人E-选择素的基本蛋白质结构和分子进化,这将有助于我们了解如何在分子水平上控制疾病和感染,并基于此知识开发特定的药物。

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