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dc.contributor.authorMarasco, Michelangelo
dc.contributor.authorCarlomagno, Teresa
dc.date.accessioned2021-07-08T12:55:02Z
dc.date.available2021-07-08T12:55:02Z
dc.date.issued2020-05-27
dc.identifier.citationJ Struct Biol X. 2020 May 27;4:100026. doi: 10.1016/j.yjsbx.2020.100026.en_US
dc.identifier.pmid32647828
dc.identifier.doi10.1016/j.yjsbx.2020.100026
dc.identifier.urihttp://hdl.handle.net/10033/622930
dc.description.abstractPhosphotyrosine (pY) signaling is instrumental to numerous cellular processes. pY recognition occurs through specialized protein modules, among which the Src-homology 2 (SH2) domain is the most common. SH2 domains are small protein modules with an invariant fold, and are present in more than a hundred proteins with different function. Here we ask the question of how such a structurally conserved, small protein domain can recognize distinct phosphopeptides with the breath of binding affinity, specificity and kinetic parameters necessary for proper control of pY-dependent signaling and rapid cellular response. We review the current knowledge on structure, thermodynamics and kinetics of SH2-phosphopeptide complexes and conclude that selective phosphopeptide recognition is governed by both structure and dynamics of the SH2 domain, as well as by the kinetics of the binding events. Further studies on the thermodynamic and kinetic properties of SH2-phosphopeptide complexes, beyond their structure, are required to understand signaling regulation.en_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.rightsAttribution 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectBinding specificityen_US
dc.subjectPhosphotyrosineen_US
dc.subjectSH2 domainen_US
dc.subjectpY signallingen_US
dc.titleSpecificity and regulation of phosphotyrosine signaling through SH2 domains.en_US
dc.typeArticleen_US
dc.identifier.eissn2590-1524
dc.contributor.departmentHZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.en_US
dc.identifier.journalJournal of structural biology: Xen_US
dc.source.volume4
dc.source.beginpage100026
dc.source.endpage
refterms.dateFOA2021-07-08T12:55:03Z
dc.source.journaltitleJournal of structural biology: X
dc.source.countryUnited States


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Attribution 4.0 International
Except where otherwise noted, this item's license is described as Attribution 4.0 International