Please use this identifier to cite or link to this item: http://hdl.handle.net/10668/3218
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dc.contributor.authorKarathanou, Konstantina-
dc.contributor.authorLazaratos, Michalis-
dc.contributor.authorBertalan, Éva-
dc.contributor.authorSiemers, Malte-
dc.contributor.authorBuzar, Krzysztof-
dc.contributor.authorSchertler, Gebhard F.X.-
dc.contributor.authordel Val, Coral-
dc.contributor.authorBondar, Ana-Nicoleta-
dc.date.accessioned2020-12-04T10:14:48Z-
dc.date.available2020-12-04T10:14:48Z-
dc.date.issued2020-09-10-
dc.identifier.citationKarathanou K, Lazaratos M, Bertalan É, Siemers M, Buzar K, Schertler GFX. A graph-based approach identifies dynamic H-bond communication networks in spike protein S of SARS-CoV-2. J Struct Biol. 2020 Nov 1;212(2):107617.es_ES
dc.identifier.issn1047-8477 (Print)es_ES
dc.identifier.otherPMC7481144es_ES
dc.identifier.urihttps://www.repositoriosalud.es/10668/10668/3218-
dc.description.abstractCorona virus spike protein S is a large homo-trimeric protein anchored in the membrane of the virion particle. Protein S binds to angiotensin-converting-enzyme 2, ACE2, of the host cell, followed by proteolysis of the spike protein, drastic protein conformational change with exposure of the fusion peptide of the virus, and entry of the virion into the host cell. The structural elements that govern conformational plasticity of the spike protein are largely unknown. Here, we present a methodology that relies upon graph and centrality analyses, augmented by bioinformatics, to identify and characterize large H-bond clusters in protein structures. We apply this methodology to protein S ectodomain and find that, in the closed conformation, the three protomers of protein S bring the same contribution to an extensive central network of H-bonds, and contribute symmetrically to a relatively large H-bond cluster at the receptor binding domain, and to a cluster near a protease cleavage site. Markedly different H-bonding at these three clusters in open and pre-fusion conformations suggest dynamic H-bond clusters could facilitate structural plasticity and selection of a protein S protomer for binding to the host receptor, and proteolytic cleavage. From analyses of spike protein sequences we identify patches of histidine and carboxylate groups that could be involved in transient proton binding.es_ES
dc.language.isoenes_ES
dc.publisherElsevier Inc.es_ES
dc.relation.ispartofJournal of Structural Biologyes_ES
dc.subjectBimolecular structurees_ES
dc.subjectHydrogen bondinges_ES
dc.subjectDynamic hydrogen-bond clusterses_ES
dc.subjectConformational plasticityes_ES
dc.subjectSARS-CoV-2 protein Ses_ES
dc.subjectACE2es_ES
dc.subjectEnlace de hidrógenoes_ES
dc.subject.meshMedical Subject Headings::Information Science::Information Science::Computing Methodologies::Algorithmses_ES
dc.subject.meshMedical Subject Headings::Disciplines and Occupations::Natural Science Disciplines::Biological Science Disciplines::Biology::Computational Biologyes_ES
dc.subject.meshMedical Subject Headings::Phenomena and Processes::Chemical Phenomena::Chemical Processes::Physicochemical Processes::Hydrogen Bondinges_ES
dc.subject.meshMedical Subject Headings::Information Science::Information Science::Computing Methodologies::Computer Graphicses_ES
dc.subject.meshMedical Subject Headings::Diseases::Virus Diseases::RNA Virus Infections::Nidovirales Infections::Coronaviridae Infections::Coronavirus Infectionses_ES
dc.subject.meshMedical Subject Headings::Organisms::Eukaryota::Animals::Chordata::Vertebrates::Mammals::Primates::Haplorhini::Catarrhini::Hominidae::Humanses_ES
dc.subject.meshMedical Subject Headings::Analytical, Diagnostic and Therapeutic Techniques and Equipment::Investigative Techniques::Models, Theoretical::Models, Moleculares_ES
dc.subject.meshMedical Subject Headings::Health Care::Environment and Public Health::Public Health::Disease Outbreaks::Epidemics::Pandemicses_ES
dc.subject.meshMedical Subject Headings::Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Hydrolases::Peptide Hydrolases::Exopeptidases::Dipeptidyl-Peptidases and Tripeptidyl-Peptidases::Peptidyl-Dipeptidase Aes_ES
dc.subject.meshMedical Subject Headings::Diseases::Virus Diseases::Pneumonia, Virales_ES
dc.subject.meshMedical Subject Headings::Phenomena and Processes::Chemical Phenomena::Biochemical Phenomena::Biochemical Processes::Protein Bindinges_ES
dc.subject.meshMedical Subject Headings::Phenomena and Processes::Chemical Phenomena::Biochemical Phenomena::Molecular Structure::Molecular Conformation::Protein Conformation::Protein Structure, Tertiary::Protein Interaction Domains and Motifses_ES
dc.subject.meshMedical Subject Headings::Analytical, Diagnostic and Therapeutic Techniques and Equipment::Investigative Techniques::Molecular Probe Techniques::Protein Interaction Mappinges_ES
dc.subject.meshMedical Subject Headings::Phenomena and Processes::Metabolic Phenomena::Metabolism::Metabolic Networks and Pathways::Protein Interaction Mapses_ES
dc.subject.meshMedical Subject Headings::Phenomena and Processes::Chemical Phenomena::Biochemical Phenomena::Molecular Structure::Molecular Conformation::Protein Conformation::Protein Structure, Quaternaryes_ES
dc.subject.meshMedical Subject Headings::Phenomena and Processes::Chemical Phenomena::Biochemical Phenomena::Molecular Structure::Molecular Conformation::Protein Conformation::Protein Structure, Secondaryes_ES
dc.subject.meshMedical Subject Headings::Chemicals and Drugs::Amino Acids, Peptides, and Proteins::Proteins::Membrane Proteins::Membrane Fusion Proteins::Viral Fusion Proteins::Spike Glycoprotein, Coronaviruses_ES
dc.subject.meshMedical Subject Headings::Phenomena and Processes::Microbiological Phenomena::Microbiological Processes::Virus Physiological Processes::Virus Internalizationes_ES
dc.titleA graph-based approach identifies dynamic H-bond communication networks in spike protein S of SARS-CoV-2es_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.description.versionYeses_ES
dc.identifier.pmid32919067es_ES
dc.rights.accessRightsAcceso abiertoes_ES
dc.identifier.doi10.1016/j.jsb.2020.107617es_ES
dc.type.versioninfo:eu-repo/semantics/publishedes_ES
dc.relation.publisherversionhttps://www.sciencedirect.com/science/article/pii/S1047847720301908?via%3Dihubes_ES
dc.contributor.authoraffiliation[Karathanou,K; Lazaratos,M; Bertalan,E; Siemers,M; Buzar,K; Bondar,AN] Freie Universität Berlin, Department of Physics, Theoretical Molecular Biophysics, Berlin, Germany. [Schertler,GFX] Paul Scherrer Institut, Department of Biology and Chemistry, Laboratory of Biomolecular Research, Villigen-PSI, Switzerland. [Schertler,GFX] ETH Zürich, Department of Biology, Zürich, Switzerland. [del Val,C] University of Granada, Department of Computer Science and Artificial Intelligence, Granada, Spain. [del Val,C] Instituto de Investigación Biosanitaria ibs.GRANADA, Granada, Spain. [del Val,C] Andalusian Research Institute in Data Science and Computational Intelligence (DaSCI Institute), Granada, Spain.es_ES
dc.relation.conferencename19 p.es_ES
dc.type.subtypeArtículo originales_ES
Appears in Collections:01- Artículos - ibsGRANADA. Instituto de Investigación Biosanitaria de Granada

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