NMR assignment of free 1H, 15N and 13C-Grb2-SH2 domain
Autor(a) principal: | |
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Data de Publicação: | 2019 |
Outros Autores: | , , |
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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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 |
|
_version_ |
1799965006161248256 |