NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state

Autores
Wang, Jing; Bains, Henrietta; Anastasia Gonzalez, Agustin; Bracken, Clay
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Brain derived neurotrophic factor (BDNF) is a member of the neurotrophin family of proteins which plays a central role in neuronal survival, growth, plasticity and memory. A single Val66Met variant has been identified in the prodomain of human BDNF that is associated with anxiety, depression and memory disorders. The structural differences within the full-length prodomain Val66 and Met66 isoforms could shed light on the mechanism of action of the Met66 and its impact on the development of neuropsychiatric-associated disorders. In the present study, we report the backbone 1H, 13C, and 15N NMR assignments of both full-length Val66 and Met66 prodomains in the presence of 2 M urea. These conditions were utilized to suppress residual structure and aid subsequent native state structural investigations aimed at mapping and identifying variant-dependent conformational differences under native-state conditions.
Fil: Wang, Jing. Weill Cornell Medical College; Estados Unidos
Fil: Bains, Henrietta. Weill Cornell Medical College; Estados Unidos
Fil: Anastasia Gonzalez, Agustin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina
Fil: Bracken, Clay. Weill Cornell Medical College; Estados Unidos
Materia
BDNF
INTRINSICALLY DISORDERED PROTEINS
NEUROTROPHIN
PRODOMAIN
UREA
VAL66MET
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/96880
Acceder
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network_name_str CONICET Digital (CONICET)
spelling NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured stateWang, JingBains, HenriettaAnastasia Gonzalez, AgustinBracken, ClayBDNFINTRINSICALLY DISORDERED PROTEINSNEUROTROPHINPRODOMAINUREAVAL66METhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Brain derived neurotrophic factor (BDNF) is a member of the neurotrophin family of proteins which plays a central role in neuronal survival, growth, plasticity and memory. A single Val66Met variant has been identified in the prodomain of human BDNF that is associated with anxiety, depression and memory disorders. The structural differences within the full-length prodomain Val66 and Met66 isoforms could shed light on the mechanism of action of the Met66 and its impact on the development of neuropsychiatric-associated disorders. In the present study, we report the backbone 1H, 13C, and 15N NMR assignments of both full-length Val66 and Met66 prodomains in the presence of 2 M urea. These conditions were utilized to suppress residual structure and aid subsequent native state structural investigations aimed at mapping and identifying variant-dependent conformational differences under native-state conditions.Fil: Wang, Jing. Weill Cornell Medical College; Estados UnidosFil: Bains, Henrietta. Weill Cornell Medical College; Estados UnidosFil: Anastasia Gonzalez, Agustin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFil: Bracken, Clay. Weill Cornell Medical College; Estados UnidosSpringer2018-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/96880Wang, Jing; Bains, Henrietta; Anastasia Gonzalez, Agustin; Bracken, Clay; NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state; Springer; Biomolecular Nmr Assignments; 12; 1; 4-2018; 43-451874-27181874-270XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1007/s12104-017-9777-0info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs12104-017-9777-0info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6865803/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:10:30Zoai:ri.conicet.gov.ar:11336/96880instacron: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 10:10:30.347CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state
title NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state
spellingShingle NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state
Wang, Jing
BDNF
INTRINSICALLY DISORDERED PROTEINS
NEUROTROPHIN
PRODOMAIN
UREA
VAL66MET
title_short NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state
title_full NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state
title_fullStr NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state
title_full_unstemmed NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state
title_sort NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state
dc.creator.none.fl_str_mv Wang, Jing
Bains, Henrietta
Anastasia Gonzalez, Agustin
Bracken, Clay
author Wang, Jing
author_facet Wang, Jing
Bains, Henrietta
Anastasia Gonzalez, Agustin
Bracken, Clay
author_role author
author2 Bains, Henrietta
Anastasia Gonzalez, Agustin
Bracken, Clay
author2_role author
author
author
dc.subject.none.fl_str_mv BDNF
INTRINSICALLY DISORDERED PROTEINS
NEUROTROPHIN
PRODOMAIN
UREA
VAL66MET
topic BDNF
INTRINSICALLY DISORDERED PROTEINS
NEUROTROPHIN
PRODOMAIN
UREA
VAL66MET
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Brain derived neurotrophic factor (BDNF) is a member of the neurotrophin family of proteins which plays a central role in neuronal survival, growth, plasticity and memory. A single Val66Met variant has been identified in the prodomain of human BDNF that is associated with anxiety, depression and memory disorders. The structural differences within the full-length prodomain Val66 and Met66 isoforms could shed light on the mechanism of action of the Met66 and its impact on the development of neuropsychiatric-associated disorders. In the present study, we report the backbone 1H, 13C, and 15N NMR assignments of both full-length Val66 and Met66 prodomains in the presence of 2 M urea. These conditions were utilized to suppress residual structure and aid subsequent native state structural investigations aimed at mapping and identifying variant-dependent conformational differences under native-state conditions.
Fil: Wang, Jing. Weill Cornell Medical College; Estados Unidos
Fil: Bains, Henrietta. Weill Cornell Medical College; Estados Unidos
Fil: Anastasia Gonzalez, Agustin. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina
Fil: Bracken, Clay. Weill Cornell Medical College; Estados Unidos
description Brain derived neurotrophic factor (BDNF) is a member of the neurotrophin family of proteins which plays a central role in neuronal survival, growth, plasticity and memory. A single Val66Met variant has been identified in the prodomain of human BDNF that is associated with anxiety, depression and memory disorders. The structural differences within the full-length prodomain Val66 and Met66 isoforms could shed light on the mechanism of action of the Met66 and its impact on the development of neuropsychiatric-associated disorders. In the present study, we report the backbone 1H, 13C, and 15N NMR assignments of both full-length Val66 and Met66 prodomains in the presence of 2 M urea. These conditions were utilized to suppress residual structure and aid subsequent native state structural investigations aimed at mapping and identifying variant-dependent conformational differences under native-state conditions.
publishDate 2018
dc.date.none.fl_str_mv 2018-04
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/11336/96880
Wang, Jing; Bains, Henrietta; Anastasia Gonzalez, Agustin; Bracken, Clay; NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state; Springer; Biomolecular Nmr Assignments; 12; 1; 4-2018; 43-45
1874-2718
1874-270X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/96880
identifier_str_mv Wang, Jing; Bains, Henrietta; Anastasia Gonzalez, Agustin; Bracken, Clay; NMR backbone resonance assignments of the prodomain variants of BDNF in the urea denatured state; Springer; Biomolecular Nmr Assignments; 12; 1; 4-2018; 43-45
1874-2718
1874-270X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1007/s12104-017-9777-0
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs12104-017-9777-0
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6865803/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
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
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score 13.13397

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