Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for microbial polysaccharides and sialylated antibody on splenic marginal zone macrophages

3 pags, 2 figs, 1 tab

Detalles Bibliográficos
Autores: Silva-Martín, Noella, Schauer, Joseph D., Park, C.G., Hermoso, Juan A.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2009
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/249288
Acceso en línea:http://hdl.handle.net/10261/249288
Access Level:acceso abierto
Palabra clave:SIGN-R1
carbohydrate-recognition domains
C-type lectin receptors
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spelling Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for microbial polysaccharides and sialylated antibody on splenic marginal zone macrophagesSilva-Martín, NoellaSchauer, Joseph D.Park, C.G.Hermoso, Juan A.SIGN-R1carbohydrate-recognition domainsC-type lectin receptors3 pags, 2 figs, 1 tabSIGN-R1, or CD209b, is a mouse C-type lectin receptor that is expressed at high levels on macrophages in lymphoid tissues, especially within the marginal zone of the spleen. SIGN-R1 can bind and mediate the uptake of various microbial polysaccharides, including dextrans, lipopolysaccharides and pneumococcal capsular polysaccharides. It has been shown that SIGN-R1 mediates the clearance of encapsulated pneumococcus, complement fixation via binding C1q independent of antibody and innate resistance to pneumococcal infection. Recently, SIGN-R1 has also been demonstrated to bind sialylated antibody and mediate its activity to suppress autoimmunity. The carbohydrate-recognition domain (CRD) of SIGN-R1 has been cloned and overexpressed in a soluble secretory form in mammalian Chinese hamster ovary (CHO) cells. The CRD protein of SIGN-R1 was purified from CHO cell-culture supernatant and concentrated for crystallization using the hanging-drop vapour-diffusion method at 291 K. Crystals grew from a mixture of 2 M ammonium sulfate in 0.1 M bis-tris pH 5.5. Single crystals, which belonged to the monoclinic space group C2 with unit-cell parameters a = 146.72, b = 92.77, c = 77.06 Å, β = 121.66°, allowed the collection of a full X-ray data set to a maximum resolution of 1.87 Å. © 2009 International Union of Crystallography All rights reserved.This work was supported by the Spanish Ministry of Education and Science (BFU2008-01711/BMC and the Factoría de Cristalización from the CONSOLIDERINGENIO 2010 program).International Union of CrystallographyMinisterio de Educación y Ciencia (España)Factoría Española de CristalizaciónConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2021202120092021info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/249288reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1107/S1744309109041992Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2492882026-05-22T06:33:51Z
dc.title.none.fl_str_mv Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for microbial polysaccharides and sialylated antibody on splenic marginal zone macrophages
title Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for microbial polysaccharides and sialylated antibody on splenic marginal zone macrophages
spellingShingle Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for microbial polysaccharides and sialylated antibody on splenic marginal zone macrophages
Silva-Martín, Noella
SIGN-R1
carbohydrate-recognition domains
C-type lectin receptors
title_short Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for microbial polysaccharides and sialylated antibody on splenic marginal zone macrophages
title_full Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for microbial polysaccharides and sialylated antibody on splenic marginal zone macrophages
title_fullStr Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for microbial polysaccharides and sialylated antibody on splenic marginal zone macrophages
title_full_unstemmed Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for microbial polysaccharides and sialylated antibody on splenic marginal zone macrophages
title_sort Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for microbial polysaccharides and sialylated antibody on splenic marginal zone macrophages
dc.creator.none.fl_str_mv Silva-Martín, Noella
Schauer, Joseph D.
Park, C.G.
Hermoso, Juan A.
author Silva-Martín, Noella
author_facet Silva-Martín, Noella
Schauer, Joseph D.
Park, C.G.
Hermoso, Juan A.
author_role author
author2 Schauer, Joseph D.
Park, C.G.
Hermoso, Juan A.
author2_role author
author
author
dc.contributor.none.fl_str_mv Ministerio de Educación y Ciencia (España)
Factoría Española de Cristalización
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv SIGN-R1
carbohydrate-recognition domains
C-type lectin receptors
topic SIGN-R1
carbohydrate-recognition domains
C-type lectin receptors
description 3 pags, 2 figs, 1 tab
publishDate 2009
dc.date.none.fl_str_mv 2009
2021
2021
2021
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/249288
url http://hdl.handle.net/10261/249288
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1107/S1744309109041992
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv International Union of Crystallography
publisher.none.fl_str_mv International Union of Crystallography
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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