{"title":"绘制SARS-CoV-2刺突蛋白S1上ACE2结合位点:分子识别模式","authors":"A. Kuznetsov, J. Järv","doi":"10.3176/proc.2020.4.09","DOIUrl":null,"url":null,"abstract":"Coronavirus SARS-CoV-2 enters the host cell via binding with the angiotensin-converting enzyme 2 (ACE2), and here we used computational modelling to study the molecular recognition pattern of this interaction The fragment of the N-terminal part of the enzyme containing amino acids 19-45 was used as the lead peptide in this study The structure of this peptide was systematically modified by successive replacement of its amino acids with alanine, serine, glycine, and phenylalanine Then docking energies were calculated for all these mutant peptides These docking energies were correlated with physical descriptors, proposed for the modelling of peptide-protein interactions, characterizing hydrophilicity and volume-related properties of amino acid side chains From these correlations the corresponding specificity factors were obtained for all amino acid positions, and thus the full description of the molecular recognition pattern of the ACE2 alpha 1 domain by the virus S1 protein binding site was obtained","PeriodicalId":54577,"journal":{"name":"Proceedings of the Estonian Academy of Sciences","volume":null,"pages":null},"PeriodicalIF":1.0000,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"3","resultStr":"{\"title\":\"Mapping the ACE2 binding site on the SARS-CoV-2 spike protein S1: molecular recognition pattern\",\"authors\":\"A. Kuznetsov, J. Järv\",\"doi\":\"10.3176/proc.2020.4.09\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Coronavirus SARS-CoV-2 enters the host cell via binding with the angiotensin-converting enzyme 2 (ACE2), and here we used computational modelling to study the molecular recognition pattern of this interaction The fragment of the N-terminal part of the enzyme containing amino acids 19-45 was used as the lead peptide in this study The structure of this peptide was systematically modified by successive replacement of its amino acids with alanine, serine, glycine, and phenylalanine Then docking energies were calculated for all these mutant peptides These docking energies were correlated with physical descriptors, proposed for the modelling of peptide-protein interactions, characterizing hydrophilicity and volume-related properties of amino acid side chains From these correlations the corresponding specificity factors were obtained for all amino acid positions, and thus the full description of the molecular recognition pattern of the ACE2 alpha 1 domain by the virus S1 protein binding site was obtained\",\"PeriodicalId\":54577,\"journal\":{\"name\":\"Proceedings of the Estonian Academy of Sciences\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":1.0000,\"publicationDate\":\"2020-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"3\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Proceedings of the Estonian Academy of Sciences\",\"FirstCategoryId\":\"103\",\"ListUrlMain\":\"https://doi.org/10.3176/proc.2020.4.09\",\"RegionNum\":4,\"RegionCategory\":\"综合性期刊\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"MULTIDISCIPLINARY SCIENCES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Proceedings of the Estonian Academy of Sciences","FirstCategoryId":"103","ListUrlMain":"https://doi.org/10.3176/proc.2020.4.09","RegionNum":4,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"MULTIDISCIPLINARY SCIENCES","Score":null,"Total":0}
Mapping the ACE2 binding site on the SARS-CoV-2 spike protein S1: molecular recognition pattern
Coronavirus SARS-CoV-2 enters the host cell via binding with the angiotensin-converting enzyme 2 (ACE2), and here we used computational modelling to study the molecular recognition pattern of this interaction The fragment of the N-terminal part of the enzyme containing amino acids 19-45 was used as the lead peptide in this study The structure of this peptide was systematically modified by successive replacement of its amino acids with alanine, serine, glycine, and phenylalanine Then docking energies were calculated for all these mutant peptides These docking energies were correlated with physical descriptors, proposed for the modelling of peptide-protein interactions, characterizing hydrophilicity and volume-related properties of amino acid side chains From these correlations the corresponding specificity factors were obtained for all amino acid positions, and thus the full description of the molecular recognition pattern of the ACE2 alpha 1 domain by the virus S1 protein binding site was obtained
期刊介绍:
The Proceedings of the Estonian Academy of Sciences is an international scientific open access journal published by the Estonian Academy of Sciences in collaboration with the University of Tartu, Tallinn University of Technology, Tallinn University, and the Estonian University of Life Sciences.
The journal publishes primary research and review papers in the English language. All articles are provided with short Estonian summaries.
All papers to be published in the journal are peer reviewed internationally.
The journal is open to word-wide scientific community for publications in all fields of science represented at the Estonian Academy of Sciences and having certain connection with our part of the world, North Europe and the Baltic area in particular.