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王瀚,赵淑玲,何九军,杨小录,周峰,侯颖春.2015.哺乳动物BMP4蛋白功能位点的进化踪迹分析.动物学杂志,50(1):21-30.
哺乳动物BMP4蛋白功能位点的进化踪迹分析
Evolutionary Trace Analysis of Functional Sites of the BMP4 Family
投稿时间:2014-05-07  修订日期:2014-12-17
DOI:DOI: 10.13859/j.cjz.201501004
中文关键词:  骨形态发生蛋白  进化踪迹分析  配基结合口袋
英文关键词:BMP4  evolutionary trace analysis  ligand-binding pockets
基金项目:陇南师专2014年重点科研项目(2014LSZK01003);
作者单位E-mail
王瀚 甘肃陇南师专农林技术学院 wanghzhangy@126.com 
赵淑玲 甘肃陇南师专农林技术学院  
何九军 甘肃陇南师专农林技术学院  
杨小录 甘肃陇南师专农林技术学院  
周峰 中国农业大学  
侯颖春 陕西师范大学生命科学学院 ychhou@snnu.edu.cn 
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中文摘要:
      摘要:哺乳动物骨形态发生蛋白(BMPs)具有促进动物软骨形成、调节细胞增殖、分化及迁移的多种功能。此外,在动物个体发育及人肿瘤的发生、发展过程中都扮演着重要角色。本文以人(Homo sapiens)源骨形态发生蛋白4(BMP4)蛋白为种子序列,利用多种生物信息学工具进行哺乳动物BMP4蛋白的序列查找及其同源蛋白的搜索,共得到具有完整结构域的同源蛋白序列72条,并以此为基础对哺乳动物BMP4的进化踪迹位点及相关的功能位点进行了比较研究。结果表明,BMP4蛋白家族的TGF?-propeptide结构域具22个全家族保守残基,而TGF-?结构域仅具84个亚家族特异性残基。人BMP4蛋白TGF-?结构域的配基结合位点主要分布于结合口袋的边缘区域。本研究为BMP4蛋白重要功能区残基的确定及未知功能位点的预测提供了重要信息。
英文摘要:
      Abstract: BMP4 is better known for its critical roles in embryonic development, mesenchymal development, organogenesis of a variety of organs and the initiation and progression of tumor. The predicted functionally important residues and 3D structure will be helpful for understanding the function of BMP4 protein and the relationship with other proteins in the BMP signal pathway. The present study aims to identify some functionally important residues and its interaction with corresponding ligands of BMP4 protein. Here, a total of 100 non-redundant protein sequences of BMP4 from various mammals were retrieved from NCBI database. Of the 100 sequences, only 72 sequences have been selected for multiple sequence alignment and the phylogentic tree was split into 10 evenly distributed partitions, namely P1-P10 in order of evolutionary time cut-off (Fig.1). Based on these results, detailed analyses on the evolutionary conservation information were performed through a variety of bioinformatics tools. Conservative analyses show that the TGF?-propeptide domain contains 22 high conservative residues. However, the TGF-? domain only contains 84 class-specific residues (Fig.3). To further explore the functional binding sites of BMP4 protein, the ligand-binding pockets were predicted using software MetaPocket 2.0. The results show that there exists three binding sites and the ligand-binding sites are surrounded the pockets (Fig.4). This study will provide useful information for identifying key residues from functional regions and predicting unknown functional sites in BMP4 family.
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