A thermodynamic analysis of the binding specificity between four human pdz domains and eight host, viral and designed ligands

Autores
Cobos, Eva S.; Sánchez Miguel, Ignacio Enrique; Chemes, Lucia Beatriz; Martinez, Jose C.; Murciano Calles, Javier
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
PDZ domains are binding modules mostly involved in cell signaling and cell–cell junctions. These domains are able to recognize a wide variety of natural targets and, among the PDZ partners, viruses have been discovered to interact with their host via a PDZ domain. With such an array of relevant and diverse interactions, PDZ binding specificity has been thoroughly studied and a traditional classification has grouped PDZ domains in three major specificity classes. In this work, we have selected four human PDZ domains covering the three canonical specificity-class binding mode and a set of their corresponding binders, including host/natural, viral and designed PDZ motifs. Through calorimetric techniques, we have covered the entire cross interactions between the selected PDZ domains and partners. The results indicate a rather basic specificity in each PDZ domain, with two of the domains that bind their cognate and some non-cognate ligands and the two other domains that basically bind their cognate partners. On the other hand, the host partners mostly bind their corresponding PDZ domain and, interestingly, the viral ligands are able to bind most of the studied PDZ domains, even those not previously described. Some viruses may have evolved to use of the ability of the PDZ fold to bind multiple targets, with resulting affinities for the virus–host interactions that are, in some cases, higher than for host–host interactions.
Fil: Cobos, Eva S.. Universidad de Granada; España
Fil: Sánchez Miguel, Ignacio Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Chemes, Lucia Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Martinez, Jose C.. Universidad de Granada; España
Fil: Murciano Calles, Javier. Universidad de Granada; España
Materia
BINDING SPECIFICITY
DIFFERENTIAL SCANNING CALORIMETRY
ISOTHERMAL TITRATION CALORIMETRY
PDZ DOMAIN
THERMODYNAMICS
VIRUS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/163566
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/163566
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A thermodynamic analysis of the binding specificity between four human pdz domains and eight host, viral and designed ligandsCobos, Eva S.Sánchez Miguel, Ignacio EnriqueChemes, Lucia BeatrizMartinez, Jose C.Murciano Calles, JavierBINDING SPECIFICITYDIFFERENTIAL SCANNING CALORIMETRYISOTHERMAL TITRATION CALORIMETRYPDZ DOMAINTHERMODYNAMICSVIRUShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1PDZ domains are binding modules mostly involved in cell signaling and cell–cell junctions. These domains are able to recognize a wide variety of natural targets and, among the PDZ partners, viruses have been discovered to interact with their host via a PDZ domain. With such an array of relevant and diverse interactions, PDZ binding specificity has been thoroughly studied and a traditional classification has grouped PDZ domains in three major specificity classes. In this work, we have selected four human PDZ domains covering the three canonical specificity-class binding mode and a set of their corresponding binders, including host/natural, viral and designed PDZ motifs. Through calorimetric techniques, we have covered the entire cross interactions between the selected PDZ domains and partners. The results indicate a rather basic specificity in each PDZ domain, with two of the domains that bind their cognate and some non-cognate ligands and the two other domains that basically bind their cognate partners. On the other hand, the host partners mostly bind their corresponding PDZ domain and, interestingly, the viral ligands are able to bind most of the studied PDZ domains, even those not previously described. Some viruses may have evolved to use of the ability of the PDZ fold to bind multiple targets, with resulting affinities for the virus–host interactions that are, in some cases, higher than for host–host interactions.Fil: Cobos, Eva S.. Universidad de Granada; EspañaFil: Sánchez Miguel, Ignacio Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Chemes, Lucia Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; ArgentinaFil: Martinez, Jose C.. Universidad de Granada; EspañaFil: Murciano Calles, Javier. Universidad de Granada; EspañaMDPI AG2021-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/163566Cobos, Eva S.; Sánchez Miguel, Ignacio Enrique; Chemes, Lucia Beatriz; Martinez, Jose C.; Murciano Calles, Javier; A thermodynamic analysis of the binding specificity between four human pdz domains and eight host, viral and designed ligands; MDPI AG; Biomolecules; 11; 8; 8-2021; 1-142218-273XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3390/biom11081071info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:11:17Zoai:ri.conicet.gov.ar:11336/163566instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:11:17.871CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A thermodynamic analysis of the binding specificity between four human pdz domains and eight host, viral and designed ligands
title A thermodynamic analysis of the binding specificity between four human pdz domains and eight host, viral and designed ligands
spellingShingle A thermodynamic analysis of the binding specificity between four human pdz domains and eight host, viral and designed ligands
Cobos, Eva S.
BINDING SPECIFICITY
DIFFERENTIAL SCANNING CALORIMETRY
ISOTHERMAL TITRATION CALORIMETRY
PDZ DOMAIN
THERMODYNAMICS
VIRUS
title_short A thermodynamic analysis of the binding specificity between four human pdz domains and eight host, viral and designed ligands
title_full A thermodynamic analysis of the binding specificity between four human pdz domains and eight host, viral and designed ligands
title_fullStr A thermodynamic analysis of the binding specificity between four human pdz domains and eight host, viral and designed ligands
title_full_unstemmed A thermodynamic analysis of the binding specificity between four human pdz domains and eight host, viral and designed ligands
title_sort A thermodynamic analysis of the binding specificity between four human pdz domains and eight host, viral and designed ligands
dc.creator.none.fl_str_mv Cobos, Eva S.
Sánchez Miguel, Ignacio Enrique
Chemes, Lucia Beatriz
Martinez, Jose C.
Murciano Calles, Javier
author Cobos, Eva S.
author_facet Cobos, Eva S.
Sánchez Miguel, Ignacio Enrique
Chemes, Lucia Beatriz
Martinez, Jose C.
Murciano Calles, Javier
author_role author
author2 Sánchez Miguel, Ignacio Enrique
Chemes, Lucia Beatriz
Martinez, Jose C.
Murciano Calles, Javier
author2_role author
author
author
author
dc.subject.none.fl_str_mv BINDING SPECIFICITY
DIFFERENTIAL SCANNING CALORIMETRY
ISOTHERMAL TITRATION CALORIMETRY
PDZ DOMAIN
THERMODYNAMICS
VIRUS
topic BINDING SPECIFICITY
DIFFERENTIAL SCANNING CALORIMETRY
ISOTHERMAL TITRATION CALORIMETRY
PDZ DOMAIN
THERMODYNAMICS
VIRUS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv PDZ domains are binding modules mostly involved in cell signaling and cell–cell junctions. These domains are able to recognize a wide variety of natural targets and, among the PDZ partners, viruses have been discovered to interact with their host via a PDZ domain. With such an array of relevant and diverse interactions, PDZ binding specificity has been thoroughly studied and a traditional classification has grouped PDZ domains in three major specificity classes. In this work, we have selected four human PDZ domains covering the three canonical specificity-class binding mode and a set of their corresponding binders, including host/natural, viral and designed PDZ motifs. Through calorimetric techniques, we have covered the entire cross interactions between the selected PDZ domains and partners. The results indicate a rather basic specificity in each PDZ domain, with two of the domains that bind their cognate and some non-cognate ligands and the two other domains that basically bind their cognate partners. On the other hand, the host partners mostly bind their corresponding PDZ domain and, interestingly, the viral ligands are able to bind most of the studied PDZ domains, even those not previously described. Some viruses may have evolved to use of the ability of the PDZ fold to bind multiple targets, with resulting affinities for the virus–host interactions that are, in some cases, higher than for host–host interactions.
Fil: Cobos, Eva S.. Universidad de Granada; España
Fil: Sánchez Miguel, Ignacio Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Chemes, Lucia Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Martinez, Jose C.. Universidad de Granada; España
Fil: Murciano Calles, Javier. Universidad de Granada; España
description PDZ domains are binding modules mostly involved in cell signaling and cell–cell junctions. These domains are able to recognize a wide variety of natural targets and, among the PDZ partners, viruses have been discovered to interact with their host via a PDZ domain. With such an array of relevant and diverse interactions, PDZ binding specificity has been thoroughly studied and a traditional classification has grouped PDZ domains in three major specificity classes. In this work, we have selected four human PDZ domains covering the three canonical specificity-class binding mode and a set of their corresponding binders, including host/natural, viral and designed PDZ motifs. Through calorimetric techniques, we have covered the entire cross interactions between the selected PDZ domains and partners. The results indicate a rather basic specificity in each PDZ domain, with two of the domains that bind their cognate and some non-cognate ligands and the two other domains that basically bind their cognate partners. On the other hand, the host partners mostly bind their corresponding PDZ domain and, interestingly, the viral ligands are able to bind most of the studied PDZ domains, even those not previously described. Some viruses may have evolved to use of the ability of the PDZ fold to bind multiple targets, with resulting affinities for the virus–host interactions that are, in some cases, higher than for host–host interactions.
publishDate 2021
dc.date.none.fl_str_mv 2021-08
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/163566
Cobos, Eva S.; Sánchez Miguel, Ignacio Enrique; Chemes, Lucia Beatriz; Martinez, Jose C.; Murciano Calles, Javier; A thermodynamic analysis of the binding specificity between four human pdz domains and eight host, viral and designed ligands; MDPI AG; Biomolecules; 11; 8; 8-2021; 1-14
2218-273X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/163566
identifier_str_mv Cobos, Eva S.; Sánchez Miguel, Ignacio Enrique; Chemes, Lucia Beatriz; Martinez, Jose C.; Murciano Calles, Javier; A thermodynamic analysis of the binding specificity between four human pdz domains and eight host, viral and designed ligands; MDPI AG; Biomolecules; 11; 8; 8-2021; 1-14
2218-273X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3390/biom11081071
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv MDPI AG
publisher.none.fl_str_mv MDPI AG
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1842270152213659648
score 13.13397

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