X-ray structure of the mature ectodomain of phogrin
- Autores
- Noguera, Martín Ezequiel; Primo, Maria Evangelina; Jakoncic, Jean; Poskus, Edgardo; Solimena, Michele; Ermacora, Mario Roberto
- Año de publicación
- 2015
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Phogrin/IA-2 and ICA512/IA-2 are two paralogs receptor-type protein-tyrosine phosphatases (RPTP) that localize in secretory granules of various neuroendocrine cells. In pancreatic islet -cells, they participate in the regulation of insulin secretion, ensuring proper granulogenesis, and -cell proliferation. The role of their cytoplasmic tail has been partially unveiled, while that of their luminal region remains unclear. To advance the understanding of its structure?function relationship, the X-ray structure of the mature ectodomain of phogrin (ME phogrin) at pH 7.4 and 4.6 has been solved at 1.95- and 2.01-Å resolution, respectively. Similarly to the ME of ICA512, ME phogrin adopts a ferredoxin-like fold: a sheet of four antiparallel -strands packed against two -helices. Sequence conservation among vertebrates, plants and insects suggests that the structural similarity extends to all the receptor family. Crystallized ME phogrin is monomeric, in agreement with solution studies but in striking contrast with the behavior of homodimeric ME ICA512. The structural details that may cause the quaternary structure differences are analyzed. The results provide a basis for building models of the overall orientation and oligomerization state of the receptor in biological membranes.
Fil: Noguera, Martín Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Primo, Maria Evangelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina
Fil: Jakoncic, Jean. Brookhaven National Laboratory; Estados Unidos
Fil: Poskus, Edgardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina
Fil: Solimena, Michele. Technische Universität Dresden.; Alemania. Max Planck Institute of Molecular Cell Biology and Genetics; Alemania
Fil: Ermacora, Mario Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina - Materia
-
STRUCTURE
PHOGRIN
IA-2
DIMER - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/102207
Ver los metadatos del registro completo
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X-ray structure of the mature ectodomain of phogrinNoguera, Martín EzequielPrimo, Maria EvangelinaJakoncic, JeanPoskus, EdgardoSolimena, MicheleErmacora, Mario RobertoSTRUCTUREPHOGRINIA-2DIMERhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Phogrin/IA-2 and ICA512/IA-2 are two paralogs receptor-type protein-tyrosine phosphatases (RPTP) that localize in secretory granules of various neuroendocrine cells. In pancreatic islet -cells, they participate in the regulation of insulin secretion, ensuring proper granulogenesis, and -cell proliferation. The role of their cytoplasmic tail has been partially unveiled, while that of their luminal region remains unclear. To advance the understanding of its structure?function relationship, the X-ray structure of the mature ectodomain of phogrin (ME phogrin) at pH 7.4 and 4.6 has been solved at 1.95- and 2.01-Å resolution, respectively. Similarly to the ME of ICA512, ME phogrin adopts a ferredoxin-like fold: a sheet of four antiparallel -strands packed against two -helices. Sequence conservation among vertebrates, plants and insects suggests that the structural similarity extends to all the receptor family. Crystallized ME phogrin is monomeric, in agreement with solution studies but in striking contrast with the behavior of homodimeric ME ICA512. The structural details that may cause the quaternary structure differences are analyzed. The results provide a basis for building models of the overall orientation and oligomerization state of the receptor in biological membranes.Fil: Noguera, Martín Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; ArgentinaFil: Primo, Maria Evangelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; ArgentinaFil: Jakoncic, Jean. Brookhaven National Laboratory; Estados UnidosFil: Poskus, Edgardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; ArgentinaFil: Solimena, Michele. Technische Universität Dresden.; Alemania. Max Planck Institute of Molecular Cell Biology and Genetics; AlemaniaFil: Ermacora, Mario Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; ArgentinaSpringer2015-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/102207Noguera, Martín Ezequiel; Primo, Maria Evangelina; Jakoncic, Jean; Poskus, Edgardo; Solimena, Michele; et al.; X-ray structure of the mature ectodomain of phogrin; Springer; Journal of Structural and Functional Genomics; 16; 1; 3-2015; 1-91345-711XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1007/s10969-014-9191-0info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs10969-014-9191-0info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:43:22Zoai:ri.conicet.gov.ar:11336/102207instacron: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:34982025-09-29 09:43:22.795CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
X-ray structure of the mature ectodomain of phogrin |
title |
X-ray structure of the mature ectodomain of phogrin |
spellingShingle |
X-ray structure of the mature ectodomain of phogrin Noguera, Martín Ezequiel STRUCTURE PHOGRIN IA-2 DIMER |
title_short |
X-ray structure of the mature ectodomain of phogrin |
title_full |
X-ray structure of the mature ectodomain of phogrin |
title_fullStr |
X-ray structure of the mature ectodomain of phogrin |
title_full_unstemmed |
X-ray structure of the mature ectodomain of phogrin |
title_sort |
X-ray structure of the mature ectodomain of phogrin |
dc.creator.none.fl_str_mv |
Noguera, Martín Ezequiel Primo, Maria Evangelina Jakoncic, Jean Poskus, Edgardo Solimena, Michele Ermacora, Mario Roberto |
author |
Noguera, Martín Ezequiel |
author_facet |
Noguera, Martín Ezequiel Primo, Maria Evangelina Jakoncic, Jean Poskus, Edgardo Solimena, Michele Ermacora, Mario Roberto |
author_role |
author |
author2 |
Primo, Maria Evangelina Jakoncic, Jean Poskus, Edgardo Solimena, Michele Ermacora, Mario Roberto |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
STRUCTURE PHOGRIN IA-2 DIMER |
topic |
STRUCTURE PHOGRIN IA-2 DIMER |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Phogrin/IA-2 and ICA512/IA-2 are two paralogs receptor-type protein-tyrosine phosphatases (RPTP) that localize in secretory granules of various neuroendocrine cells. In pancreatic islet -cells, they participate in the regulation of insulin secretion, ensuring proper granulogenesis, and -cell proliferation. The role of their cytoplasmic tail has been partially unveiled, while that of their luminal region remains unclear. To advance the understanding of its structure?function relationship, the X-ray structure of the mature ectodomain of phogrin (ME phogrin) at pH 7.4 and 4.6 has been solved at 1.95- and 2.01-Å resolution, respectively. Similarly to the ME of ICA512, ME phogrin adopts a ferredoxin-like fold: a sheet of four antiparallel -strands packed against two -helices. Sequence conservation among vertebrates, plants and insects suggests that the structural similarity extends to all the receptor family. Crystallized ME phogrin is monomeric, in agreement with solution studies but in striking contrast with the behavior of homodimeric ME ICA512. The structural details that may cause the quaternary structure differences are analyzed. The results provide a basis for building models of the overall orientation and oligomerization state of the receptor in biological membranes. Fil: Noguera, Martín Ezequiel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina Fil: Primo, Maria Evangelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina Fil: Jakoncic, Jean. Brookhaven National Laboratory; Estados Unidos Fil: Poskus, Edgardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni; Argentina Fil: Solimena, Michele. Technische Universität Dresden.; Alemania. Max Planck Institute of Molecular Cell Biology and Genetics; Alemania Fil: Ermacora, Mario Roberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto Multidisciplinario de Biología Celular. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Instituto Multidisciplinario de Biología Celular. Universidad Nacional de La Plata. Instituto Multidisciplinario de Biología Celular; Argentina |
description |
Phogrin/IA-2 and ICA512/IA-2 are two paralogs receptor-type protein-tyrosine phosphatases (RPTP) that localize in secretory granules of various neuroendocrine cells. In pancreatic islet -cells, they participate in the regulation of insulin secretion, ensuring proper granulogenesis, and -cell proliferation. The role of their cytoplasmic tail has been partially unveiled, while that of their luminal region remains unclear. To advance the understanding of its structure?function relationship, the X-ray structure of the mature ectodomain of phogrin (ME phogrin) at pH 7.4 and 4.6 has been solved at 1.95- and 2.01-Å resolution, respectively. Similarly to the ME of ICA512, ME phogrin adopts a ferredoxin-like fold: a sheet of four antiparallel -strands packed against two -helices. Sequence conservation among vertebrates, plants and insects suggests that the structural similarity extends to all the receptor family. Crystallized ME phogrin is monomeric, in agreement with solution studies but in striking contrast with the behavior of homodimeric ME ICA512. The structural details that may cause the quaternary structure differences are analyzed. The results provide a basis for building models of the overall orientation and oligomerization state of the receptor in biological membranes. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-03 |
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/11336/102207 Noguera, Martín Ezequiel; Primo, Maria Evangelina; Jakoncic, Jean; Poskus, Edgardo; Solimena, Michele; et al.; X-ray structure of the mature ectodomain of phogrin; Springer; Journal of Structural and Functional Genomics; 16; 1; 3-2015; 1-9 1345-711X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/102207 |
identifier_str_mv |
Noguera, Martín Ezequiel; Primo, Maria Evangelina; Jakoncic, Jean; Poskus, Edgardo; Solimena, Michele; et al.; X-ray structure of the mature ectodomain of phogrin; Springer; Journal of Structural and Functional Genomics; 16; 1; 3-2015; 1-9 1345-711X 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/s10969-014-9191-0 info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007%2Fs10969-014-9191-0 |
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 application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Springer |
publisher.none.fl_str_mv |
Springer |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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