NMR assignment of free 1H, 15N and 13C-Grb2-SH2 domain

Detalhes bibliográficos
Autor(a) principal: Sanches, Karoline [UNESP]
Data de Publicação: 2019
Outros Autores: Caruso, Ícaro P. [UNESP], Almeida, Fábio C. L., Melo, Fernando A. [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1007/s12104-019-09894-x
http://hdl.handle.net/11449/187620
Resumo: Growth factor receptor-bound protein 2 (Grb2) is an adaptor protein composed of three domains, an N-terminal SH3 (nSH3), SH2 and a C-terminal SH3 (cSH3) domains. This multi-domain protein has been reported to be a key factor in many signaling pathways related to controlling cell survival, differentiation, and growth. The Grb2-SH2 domain has been a focus for the study of the interaction with peptides and small molecules to act as inhibitors in uncontrolled cell growth, and consequently inhibit tumor proliferation. Here we describe the almost complete assignment of the free SH2 domain at pH 7. This work prepares the ground for further structural studies, backbone dynamics, mapping of interactions and drug screening and development. TalosN secondary structure prediction showed great similarity with the available structures in the PDB.
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spelling NMR assignment of free 1H, 15N and 13C-Grb2-SH2 domainAssignmentGrb2Isotopic labeledNMRSH2 domainGrowth factor receptor-bound protein 2 (Grb2) is an adaptor protein composed of three domains, an N-terminal SH3 (nSH3), SH2 and a C-terminal SH3 (cSH3) domains. This multi-domain protein has been reported to be a key factor in many signaling pathways related to controlling cell survival, differentiation, and growth. The Grb2-SH2 domain has been a focus for the study of the interaction with peptides and small molecules to act as inhibitors in uncontrolled cell growth, and consequently inhibit tumor proliferation. Here we describe the almost complete assignment of the free SH2 domain at pH 7. This work prepares the ground for further structural studies, backbone dynamics, mapping of interactions and drug screening and development. TalosN secondary structure prediction showed great similarity with the available structures in the PDB.Universidade Estadual PaulistaFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Fundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Multiuser Center for Biomolecular Innovation (CMIB) Department of Physics São Paulo State University (UNESP)Institute of Medical Biochemistry (IBqM) and National Center of Nuclear Magnetic Resonance (CNRMN) Center for Structural Biology and Bioimaging (CENABIO) Federal University of Rio de JaneiroMultiuser Center for Biomolecular Innovation (CMIB) Department of Physics São Paulo State University (UNESP)Universidade Estadual Paulista: 09/2017Universidade Estadual Paulista: 12/2017FAPESP: 2009/53989-4FAPESP: 2014/17630-0FAPESP: 2017/20642-8FAPERJ: 204432FAPERJ: 239229CNPq: 309564/2017-4CNPq: 442951/2014-0Universidade Estadual Paulista (Unesp)Federal University of Rio de JaneiroSanches, Karoline [UNESP]Caruso, Ícaro P. [UNESP]Almeida, Fábio C. L.Melo, Fernando A. [UNESP]2019-10-06T15:42:02Z2019-10-06T15:42:02Z2019-10-15info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article295-298http://dx.doi.org/10.1007/s12104-019-09894-xBiomolecular NMR Assignments, v. 13, n. 2, p. 295-298, 2019.1874-270X1874-2718http://hdl.handle.net/11449/18762010.1007/s12104-019-09894-x2-s2.0-85065172205Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBiomolecular NMR Assignmentsinfo:eu-repo/semantics/openAccess2021-10-23T20:19:23Zoai:repositorio.unesp.br:11449/187620Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462021-10-23T20:19:23Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv NMR assignment of free 1H, 15N and 13C-Grb2-SH2 domain
title NMR assignment of free 1H, 15N and 13C-Grb2-SH2 domain
spellingShingle NMR assignment of free 1H, 15N and 13C-Grb2-SH2 domain
Sanches, Karoline [UNESP]
Assignment
Grb2
Isotopic labeled
NMR
SH2 domain
title_short NMR assignment of free 1H, 15N and 13C-Grb2-SH2 domain
title_full NMR assignment of free 1H, 15N and 13C-Grb2-SH2 domain
title_fullStr NMR assignment of free 1H, 15N and 13C-Grb2-SH2 domain
title_full_unstemmed NMR assignment of free 1H, 15N and 13C-Grb2-SH2 domain
title_sort NMR assignment of free 1H, 15N and 13C-Grb2-SH2 domain
author Sanches, Karoline [UNESP]
author_facet Sanches, Karoline [UNESP]
Caruso, Ícaro P. [UNESP]
Almeida, Fábio C. L.
Melo, Fernando A. [UNESP]
author_role author
author2 Caruso, Ícaro P. [UNESP]
Almeida, Fábio C. L.
Melo, Fernando A. [UNESP]
author2_role author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
Federal University of Rio de Janeiro
dc.contributor.author.fl_str_mv Sanches, Karoline [UNESP]
Caruso, Ícaro P. [UNESP]
Almeida, Fábio C. L.
Melo, Fernando A. [UNESP]
dc.subject.por.fl_str_mv Assignment
Grb2
Isotopic labeled
NMR
SH2 domain
topic Assignment
Grb2
Isotopic labeled
NMR
SH2 domain
description Growth factor receptor-bound protein 2 (Grb2) is an adaptor protein composed of three domains, an N-terminal SH3 (nSH3), SH2 and a C-terminal SH3 (cSH3) domains. This multi-domain protein has been reported to be a key factor in many signaling pathways related to controlling cell survival, differentiation, and growth. The Grb2-SH2 domain has been a focus for the study of the interaction with peptides and small molecules to act as inhibitors in uncontrolled cell growth, and consequently inhibit tumor proliferation. Here we describe the almost complete assignment of the free SH2 domain at pH 7. This work prepares the ground for further structural studies, backbone dynamics, mapping of interactions and drug screening and development. TalosN secondary structure prediction showed great similarity with the available structures in the PDB.
publishDate 2019
dc.date.none.fl_str_mv 2019-10-06T15:42:02Z
2019-10-06T15:42:02Z
2019-10-15
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1007/s12104-019-09894-x
Biomolecular NMR Assignments, v. 13, n. 2, p. 295-298, 2019.
1874-270X
1874-2718
http://hdl.handle.net/11449/187620
10.1007/s12104-019-09894-x
2-s2.0-85065172205
url http://dx.doi.org/10.1007/s12104-019-09894-x
http://hdl.handle.net/11449/187620
identifier_str_mv Biomolecular NMR Assignments, v. 13, n. 2, p. 295-298, 2019.
1874-270X
1874-2718
10.1007/s12104-019-09894-x
2-s2.0-85065172205
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Biomolecular NMR Assignments
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 295-298
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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