Crystal Structure of the C-type Lectin-like Domain from the Human Hematopoietic Cell Receptor CD69

Autores
Llera, Andrea Sabina; Viedma, Fernando; Sánchez Madrid, Francisco; Tormo, José
Año de publicación
2001
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
CD69, one of the earliest specific antigens acquired during lymphoid activation, acts as a signal-transducing receptor involved in cellular activation events, including proliferation and induction of specific genes. CD69 belongs to a family of receptors that modulate the immune response and whose genes are clustered in the natural killer (NK) gene complex. The extracellular portion of these receptors represent a subfamily of C-type lectin-like domains (CTLDs), which are divergent from true C-type lectins and are referred to as NK-cell domains (NKDs). We have determined the three-dimensional structure of human CD69 NKD in two different crystal forms. CD69 NKD adopts the canonical CTLD fold but lacks the features involved in Ca(2+) and carbohydrate binding by C-type lectins. CD69 NKD dimerizes noncovalently, both in solution and in crystalline state. The dimer interface consists of a hydrophobic, loosely packed core, surrounded by polar interactions, including an interdomain beta sheet. The intersubunit core shows certain structural plasticity that may facilitate conformational rearrangements for binding to ligands. The surface equivalent to the binding site of other members of the CTLD superfamily reveals a hydrophobic patch surrounded by conserved charged residues that probably constitutes the CD69 ligand-binding site.
Fil: Llera, Andrea Sabina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Viedma, Fernando. Universidad Autónoma de Madrid; España
Fil: Sánchez Madrid, Francisco. Universidad Autónoma de Madrid; España
Fil: Tormo, José. Universidad Autónoma de Madrid; España
Materia
ANTIGENS
SIGNAL TRANSDUCTION
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:11336/45350
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/45350
network_acronym_str CONICETDig
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network_name_str CONICET Digital (CONICET)
spelling Crystal Structure of the C-type Lectin-like Domain from the Human Hematopoietic Cell Receptor CD69Llera, Andrea SabinaViedma, FernandoSánchez Madrid, FranciscoTormo, JoséANTIGENSSIGNAL TRANSDUCTIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1CD69, one of the earliest specific antigens acquired during lymphoid activation, acts as a signal-transducing receptor involved in cellular activation events, including proliferation and induction of specific genes. CD69 belongs to a family of receptors that modulate the immune response and whose genes are clustered in the natural killer (NK) gene complex. The extracellular portion of these receptors represent a subfamily of C-type lectin-like domains (CTLDs), which are divergent from true C-type lectins and are referred to as NK-cell domains (NKDs). We have determined the three-dimensional structure of human CD69 NKD in two different crystal forms. CD69 NKD adopts the canonical CTLD fold but lacks the features involved in Ca(2+) and carbohydrate binding by C-type lectins. CD69 NKD dimerizes noncovalently, both in solution and in crystalline state. The dimer interface consists of a hydrophobic, loosely packed core, surrounded by polar interactions, including an interdomain beta sheet. The intersubunit core shows certain structural plasticity that may facilitate conformational rearrangements for binding to ligands. The surface equivalent to the binding site of other members of the CTLD superfamily reveals a hydrophobic patch surrounded by conserved charged residues that probably constitutes the CD69 ligand-binding site.Fil: Llera, Andrea Sabina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Viedma, Fernando. Universidad Autónoma de Madrid; EspañaFil: Sánchez Madrid, Francisco. Universidad Autónoma de Madrid; EspañaFil: Tormo, José. Universidad Autónoma de Madrid; EspañaAmerican Society for Biochemistry and Molecular Biology2001-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/45350Llera, Andrea Sabina; Viedma, Fernando; Sánchez Madrid, Francisco; Tormo, José; Crystal Structure of the C-type Lectin-like Domain from the Human Hematopoietic Cell Receptor CD69; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 276; 10; 3-2001; 7312-73190021-92581083-351XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/276/10/7312.longinfo:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M008573200info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:50:47Zoai:ri.conicet.gov.ar:11336/45350instacron: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 09:50:48.229CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Crystal Structure of the C-type Lectin-like Domain from the Human Hematopoietic Cell Receptor CD69
title Crystal Structure of the C-type Lectin-like Domain from the Human Hematopoietic Cell Receptor CD69
spellingShingle Crystal Structure of the C-type Lectin-like Domain from the Human Hematopoietic Cell Receptor CD69
Llera, Andrea Sabina
ANTIGENS
SIGNAL TRANSDUCTION
title_short Crystal Structure of the C-type Lectin-like Domain from the Human Hematopoietic Cell Receptor CD69
title_full Crystal Structure of the C-type Lectin-like Domain from the Human Hematopoietic Cell Receptor CD69
title_fullStr Crystal Structure of the C-type Lectin-like Domain from the Human Hematopoietic Cell Receptor CD69
title_full_unstemmed Crystal Structure of the C-type Lectin-like Domain from the Human Hematopoietic Cell Receptor CD69
title_sort Crystal Structure of the C-type Lectin-like Domain from the Human Hematopoietic Cell Receptor CD69
dc.creator.none.fl_str_mv Llera, Andrea Sabina
Viedma, Fernando
Sánchez Madrid, Francisco
Tormo, José
author Llera, Andrea Sabina
author_facet Llera, Andrea Sabina
Viedma, Fernando
Sánchez Madrid, Francisco
Tormo, José
author_role author
author2 Viedma, Fernando
Sánchez Madrid, Francisco
Tormo, José
author2_role author
author
author
dc.subject.none.fl_str_mv ANTIGENS
SIGNAL TRANSDUCTION
topic ANTIGENS
SIGNAL TRANSDUCTION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv CD69, one of the earliest specific antigens acquired during lymphoid activation, acts as a signal-transducing receptor involved in cellular activation events, including proliferation and induction of specific genes. CD69 belongs to a family of receptors that modulate the immune response and whose genes are clustered in the natural killer (NK) gene complex. The extracellular portion of these receptors represent a subfamily of C-type lectin-like domains (CTLDs), which are divergent from true C-type lectins and are referred to as NK-cell domains (NKDs). We have determined the three-dimensional structure of human CD69 NKD in two different crystal forms. CD69 NKD adopts the canonical CTLD fold but lacks the features involved in Ca(2+) and carbohydrate binding by C-type lectins. CD69 NKD dimerizes noncovalently, both in solution and in crystalline state. The dimer interface consists of a hydrophobic, loosely packed core, surrounded by polar interactions, including an interdomain beta sheet. The intersubunit core shows certain structural plasticity that may facilitate conformational rearrangements for binding to ligands. The surface equivalent to the binding site of other members of the CTLD superfamily reveals a hydrophobic patch surrounded by conserved charged residues that probably constitutes the CD69 ligand-binding site.
Fil: Llera, Andrea Sabina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Viedma, Fernando. Universidad Autónoma de Madrid; España
Fil: Sánchez Madrid, Francisco. Universidad Autónoma de Madrid; España
Fil: Tormo, José. Universidad Autónoma de Madrid; España
description CD69, one of the earliest specific antigens acquired during lymphoid activation, acts as a signal-transducing receptor involved in cellular activation events, including proliferation and induction of specific genes. CD69 belongs to a family of receptors that modulate the immune response and whose genes are clustered in the natural killer (NK) gene complex. The extracellular portion of these receptors represent a subfamily of C-type lectin-like domains (CTLDs), which are divergent from true C-type lectins and are referred to as NK-cell domains (NKDs). We have determined the three-dimensional structure of human CD69 NKD in two different crystal forms. CD69 NKD adopts the canonical CTLD fold but lacks the features involved in Ca(2+) and carbohydrate binding by C-type lectins. CD69 NKD dimerizes noncovalently, both in solution and in crystalline state. The dimer interface consists of a hydrophobic, loosely packed core, surrounded by polar interactions, including an interdomain beta sheet. The intersubunit core shows certain structural plasticity that may facilitate conformational rearrangements for binding to ligands. The surface equivalent to the binding site of other members of the CTLD superfamily reveals a hydrophobic patch surrounded by conserved charged residues that probably constitutes the CD69 ligand-binding site.
publishDate 2001
dc.date.none.fl_str_mv 2001-03
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/11336/45350
Llera, Andrea Sabina; Viedma, Fernando; Sánchez Madrid, Francisco; Tormo, José; Crystal Structure of the C-type Lectin-like Domain from the Human Hematopoietic Cell Receptor CD69; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 276; 10; 3-2001; 7312-7319
0021-9258
1083-351X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/45350
identifier_str_mv Llera, Andrea Sabina; Viedma, Fernando; Sánchez Madrid, Francisco; Tormo, José; Crystal Structure of the C-type Lectin-like Domain from the Human Hematopoietic Cell Receptor CD69; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 276; 10; 3-2001; 7312-7319
0021-9258
1083-351X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/276/10/7312.long
info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M008573200
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
dc.publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
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 13.070432

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