IN SILICO CHARACTERIZATION OF HUMAN INTERFERON ALPHA/BETA RECEPTOR 2 (ISOFORM A, B AND C) PROTEIN

PAFMJ Pub Date : 2021-12-31 DOI:10.51253/pafmj.v71i6.6571
Ambreen Javed, G. Trali, Hassan Burair Abbas, A. Sadiq
{"title":"IN SILICO CHARACTERIZATION OF HUMAN INTERFERON ALPHA/BETA RECEPTOR 2 (ISOFORM A, B AND C) PROTEIN","authors":"Ambreen Javed, G. Trali, Hassan Burair Abbas, A. Sadiq","doi":"10.51253/pafmj.v71i6.6571","DOIUrl":null,"url":null,"abstract":"Objective: To predict the tertiary structure of human interferon alpha/beta receptor 2 protein. \nStudy Design: Structure prediction by using bio informatics tools. \nPlace and Duration of Study: Department of Biochemistry, Swat Medical College (STMC), Saidu Shareef, Swat, Pakistan, from Aug 2019 to Dec 2019. \nMethodology: All protein sequences of human interferon alpha/beta receptor 2 (isoforma, b and c) (IFNAR-2) were retrieved through the BLAST search (The Basic Local Alignment Search Tool) from available databases ‘NCBI’ (National Centre for Biotechnology Information) and ‘Uni Prot KB’ (The Universal Protein Resource). Sequence alignment was conducted by using Clustal Omega, to get the consensus sequence for IFNAR-2 protein. Consensus protein sequence of human IFNAR-2 was used for the prediction of the three-dimensional structure by employing Swiss-Model Server. Moreover, subcellular localization analysis was also performed by using CELLO2GO program. \nResults: Structural model of human IFNAR-2 protein was predicted and evaluated by Ramachandran dimension. Cellular localization of tertiary topological domains of the predicted models were revealed probability of localization of IFNAR-2 protein (isoform a, b & c) is highest in the plasma membrane due to the presence of the transmembrane alpha helical regions. \nConclusion: This study predicted the tertiary structural dimensions of human IFNAR-2 protein, including the specific topological domains that contribute towards the subcellular compartmentalization and functional characteristics.","PeriodicalId":19982,"journal":{"name":"PAFMJ","volume":"50 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2021-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"PAFMJ","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.51253/pafmj.v71i6.6571","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

Objective: To predict the tertiary structure of human interferon alpha/beta receptor 2 protein. Study Design: Structure prediction by using bio informatics tools. Place and Duration of Study: Department of Biochemistry, Swat Medical College (STMC), Saidu Shareef, Swat, Pakistan, from Aug 2019 to Dec 2019. Methodology: All protein sequences of human interferon alpha/beta receptor 2 (isoforma, b and c) (IFNAR-2) were retrieved through the BLAST search (The Basic Local Alignment Search Tool) from available databases ‘NCBI’ (National Centre for Biotechnology Information) and ‘Uni Prot KB’ (The Universal Protein Resource). Sequence alignment was conducted by using Clustal Omega, to get the consensus sequence for IFNAR-2 protein. Consensus protein sequence of human IFNAR-2 was used for the prediction of the three-dimensional structure by employing Swiss-Model Server. Moreover, subcellular localization analysis was also performed by using CELLO2GO program. Results: Structural model of human IFNAR-2 protein was predicted and evaluated by Ramachandran dimension. Cellular localization of tertiary topological domains of the predicted models were revealed probability of localization of IFNAR-2 protein (isoform a, b & c) is highest in the plasma membrane due to the presence of the transmembrane alpha helical regions. Conclusion: This study predicted the tertiary structural dimensions of human IFNAR-2 protein, including the specific topological domains that contribute towards the subcellular compartmentalization and functional characteristics.
人干扰素α / β受体2(异构体a、b和c)蛋白的计算机表征
目的:预测人干扰素α / β受体2蛋白的三级结构。研究设计:利用生物信息学工具进行结构预测。学习地点和时间:2019年8月至2019年12月,巴基斯坦斯瓦特,斯瓦特医学院(STMC)生物化学系。方法:通过BLAST搜索(基本局部比对搜索工具)从NCBI(国家生物技术信息中心)和Uni Prot KB(通用蛋白质资源)数据库中检索人干扰素α / β受体2(异构体,b和c) (IFNAR-2)的所有蛋白质序列。利用Clustal Omega进行序列比对,得到IFNAR-2蛋白的一致序列。采用Swiss-Model Server软件对人IFNAR-2的一致蛋白序列进行三维结构预测。利用CELLO2GO程序进行亚细胞定位分析。结果:用Ramachandran维数预测并评价了人IFNAR-2蛋白的结构模型。预测模型的三级拓扑结构域的细胞定位显示,由于存在跨膜α螺旋区,IFNAR-2蛋白(异构体a, b和c)在质膜中的定位概率最高。结论:本研究预测了人IFNAR-2蛋白的三级结构维度,包括与亚细胞区隔和功能特征有关的特定拓扑结构域。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信