Evidence for conserved fuzzy complexes involving a preorganized Unique domain in the Src family of kinases

The N-terminal regulatory region of c-Src including the SH4, Unique and SH3 domains adopts a compact, yet highly dynamic, structure that can be described as an intramolecular fuzzy complex. Most of the long-range interactions within the Unique domain are also observed in constructs lacking the struc...

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Autores: Arbesú Andrés, Miguel, Maffei, Mariano, 1985-, Cordeiro, Tiago N., Teixeira, Joao M. C., Pérez, Yolanda, Bernadó Peretó, Pau, Roche, Serge, Pons Vallès, Miquel
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2017
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/109624
Acceso en línea:https://hdl.handle.net/2445/109624
Access Level:acceso abierto
Palabra clave:Proteïnes quinases
Bioquímica
Protein kinases
Biochemistry
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spelling Evidence for conserved fuzzy complexes involving a preorganized Unique domain in the Src family of kinasesArbesú Andrés, MiguelMaffei, Mariano, 1985-Cordeiro, Tiago N.Teixeira, Joao M. C.Pérez, YolandaBernadó Peretó, PauRoche, SergePons Vallès, MiquelProteïnes quinasesBioquímicaProtein kinasesBiochemistryThe N-terminal regulatory region of c-Src including the SH4, Unique and SH3 domains adopts a compact, yet highly dynamic, structure that can be described as an intramolecular fuzzy complex. Most of the long-range interactions within the Unique domain are also observed in constructs lacking the structured SH3, indicating a considerable degree of preorganization of the disordered Unique domain. Here we report that members of the Src family of kinases (SFK) share well-conserved sequence features involving aromatic residues in their Unique domains. This observation contrasts with the supposed lack of sequence homology implied by the name of these domains and suggests that the other members of SFK also have a regulatory region involving their Unique domains. We argue that the Unique domain of each SFK is sensitive to specific input signals, encoded by each specific sequence, but the entire family shares a common mechanism for connecting the disordered and structured domains.Elsevier B.V.2017201820172017info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersion20 p.application/pdfhttps://hdl.handle.net/2445/109624Articles publicats en revistes (Química Inorgànica i Orgànica)reponame:Recercat. Dipósit de la Recerca de Catalunyainstname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)InglésVersió postprint del document publicat a: https://doi.org/10.17632/t2by82c3rr.2Structure, 2017, vol. 25, p. 630-640https://doi.org/10.17632/t2by82c3rr.2cc-by-nc-nd (c) Elsevier B.V., 2017http://creativecommons.org/licenses/by-nc-nd/3.0/esinfo:eu-repo/semantics/openAccessoai:recercat.cat:2445/1096242026-05-29T05:05:01Z
dc.title.none.fl_str_mv Evidence for conserved fuzzy complexes involving a preorganized Unique domain in the Src family of kinases
title Evidence for conserved fuzzy complexes involving a preorganized Unique domain in the Src family of kinases
spellingShingle Evidence for conserved fuzzy complexes involving a preorganized Unique domain in the Src family of kinases
Arbesú Andrés, Miguel
Proteïnes quinases
Bioquímica
Protein kinases
Biochemistry
title_short Evidence for conserved fuzzy complexes involving a preorganized Unique domain in the Src family of kinases
title_full Evidence for conserved fuzzy complexes involving a preorganized Unique domain in the Src family of kinases
title_fullStr Evidence for conserved fuzzy complexes involving a preorganized Unique domain in the Src family of kinases
title_full_unstemmed Evidence for conserved fuzzy complexes involving a preorganized Unique domain in the Src family of kinases
title_sort Evidence for conserved fuzzy complexes involving a preorganized Unique domain in the Src family of kinases
dc.creator.none.fl_str_mv Arbesú Andrés, Miguel
Maffei, Mariano, 1985-
Cordeiro, Tiago N.
Teixeira, Joao M. C.
Pérez, Yolanda
Bernadó Peretó, Pau
Roche, Serge
Pons Vallès, Miquel
author Arbesú Andrés, Miguel
author_facet Arbesú Andrés, Miguel
Maffei, Mariano, 1985-
Cordeiro, Tiago N.
Teixeira, Joao M. C.
Pérez, Yolanda
Bernadó Peretó, Pau
Roche, Serge
Pons Vallès, Miquel
author_role author
author2 Maffei, Mariano, 1985-
Cordeiro, Tiago N.
Teixeira, Joao M. C.
Pérez, Yolanda
Bernadó Peretó, Pau
Roche, Serge
Pons Vallès, Miquel
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Proteïnes quinases
Bioquímica
Protein kinases
Biochemistry
topic Proteïnes quinases
Bioquímica
Protein kinases
Biochemistry
description The N-terminal regulatory region of c-Src including the SH4, Unique and SH3 domains adopts a compact, yet highly dynamic, structure that can be described as an intramolecular fuzzy complex. Most of the long-range interactions within the Unique domain are also observed in constructs lacking the structured SH3, indicating a considerable degree of preorganization of the disordered Unique domain. Here we report that members of the Src family of kinases (SFK) share well-conserved sequence features involving aromatic residues in their Unique domains. This observation contrasts with the supposed lack of sequence homology implied by the name of these domains and suggests that the other members of SFK also have a regulatory region involving their Unique domains. We argue that the Unique domain of each SFK is sensitive to specific input signals, encoded by each specific sequence, but the entire family shares a common mechanism for connecting the disordered and structured domains.
publishDate 2017
dc.date.none.fl_str_mv 2017
2017
2017
2018
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/109624
url https://hdl.handle.net/2445/109624
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Versió postprint del document publicat a: https://doi.org/10.17632/t2by82c3rr.2
Structure, 2017, vol. 25, p. 630-640
https://doi.org/10.17632/t2by82c3rr.2
dc.rights.none.fl_str_mv cc-by-nc-nd (c) Elsevier B.V., 2017
http://creativecommons.org/licenses/by-nc-nd/3.0/es
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by-nc-nd (c) Elsevier B.V., 2017
http://creativecommons.org/licenses/by-nc-nd/3.0/es
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 20 p.
application/pdf
dc.publisher.none.fl_str_mv Elsevier B.V.
publisher.none.fl_str_mv Elsevier B.V.
dc.source.none.fl_str_mv Articles publicats en revistes (Química Inorgànica i Orgànica)
reponame:Recercat. Dipósit de la Recerca de Catalunya
instname:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
instname_str Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
reponame_str Recercat. Dipósit de la Recerca de Catalunya
collection Recercat. Dipósit de la Recerca de Catalunya
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.81155

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