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Understanding binding affinity and specificity of modular protein domains: A focus in ligand design for the polyproline-binding families

dc.contributor.authorMartínez Herrerías, José Cristóbal 
dc.contributor.authorCastillo, Francisco
dc.contributor.authorRuiz Sanz, Javier 
dc.contributor.authorMurciano Calles, Javier 
dc.contributor.authorCámara-Artigas, Ana
dc.contributor.authorLuque Fernández, Irene 
dc.date.accessioned2025-01-22T09:43:30Z
dc.date.available2025-01-22T09:43:30Z
dc.date.issued2022-01-10
dc.identifier.citationMartinez JC, Castillo F, Ruiz-Sanz J, Murciano-Calles J, Camara-Artigas A, Luque I. Understanding binding affinity and specificity of modular protein domains: A focus in ligand design for the polyproline-binding families. Adv Protein Chem Struct Biol. 2022;130:161-188. doi: 10.1016/bs.apcsb.2021.12.002. Epub 2022 Jan 10. PMID: 35534107.es_ES
dc.identifier.urihttps://hdl.handle.net/10481/99939
dc.description.abstractWithin the modular protein domains there are five families that recognize proline-rich sequences: SH3, WW, EVH1, GYF and UEV domains. This chapter reviews the main strategies developed for the design of ligands for these families, including peptides, peptidomimetics and drugs. We also describe some studies aimed to understand the molecular reasons responsible for the intrinsic affinity and specificity of these domains.es_ES
dc.language.isoenges_ES
dc.publisherElsevier Inc.es_ES
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectEVH1 domains; GYF domainses_ES
dc.subjectLigand designes_ES
dc.subjectPolyproline peptideses_ES
dc.subjectProtein-protein interactionses_ES
dc.subjectSH3 domainses_ES
dc.subjectStructure/function relationships in protein domainses_ES
dc.subjectUEV domains; WW domainses_ES
dc.titleUnderstanding binding affinity and specificity of modular protein domains: A focus in ligand design for the polyproline-binding familieses_ES
dc.typebook partes_ES
dc.rights.accessRightsopen accesses_ES
dc.identifier.doihttps://doi.org/10.1016/BS.APCSB.2021.12.002
dc.type.hasVersionAMes_ES


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Attribution-NonCommercial-NoDerivatives 4.0 Internacional
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