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dc.contributor.authorKarathanou, Konstantina
dc.contributor.authorLazaratos, Michalis
dc.contributor.authorVal Muñoz, María Coral Del 
dc.date.accessioned2020-11-12T11:54:00Z
dc.date.available2020-11-12T11:54:00Z
dc.date.issued2020-09-10
dc.identifier.citationK. Karathanou, et al. A graph-based approach identifies dynamic H-bond communication networks in spike protein S of SARS-CoV-2. Journal of Structural Biology 212 (2020) 107617 [https://doi.org/10.1016/j.jsb.2020.107617]es_ES
dc.identifier.urihttp://hdl.handle.net/10481/64227
dc.descriptionWe apply graph-based approaches to identify H-bond clusters in protein complexes. Three conformations of spike protein S have distinct H-bond clusters at key sites. Hydrogen-bond clusters could govern structural plasticity of spike protein S. Protein S binds to ACE2 receptor via H-bond clusters extending deep across interface.es_ES
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.description.sponsorshipPSI COVID19 Emergency Science Fundes_ES
dc.description.sponsorshipSpanish Ministry of Science, Innovation and Universities RTI2018-098983-B-I00es_ES
dc.description.sponsorshipExcellence Initiative of the German Federal and State Governments via the Freie Universitat Berlines_ES
dc.description.sponsorshipGerman Research Foundation (DFG) SFB 1078es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.rightsAtribución-NoComercial-SinDerivadas 3.0 España*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/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.subjectCOVID-19es_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.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES
dc.identifier.doi10.1016/j.jsb.2020.107617
dc.type.hasVersioninfo:eu-repo/semantics/publishedVersiones_ES


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