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dc.contributor.author
Sundberg, Eric J.
dc.contributor.author
Li, Hongmin
dc.contributor.author
Llera, Andrea Sabina
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McCormick, John K.
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Tormo, José
dc.contributor.author
Schlievert, Patrick M.
dc.contributor.author
Karjalainen, Klaus
dc.contributor.author
Mariuzza, Roy A.
dc.date.available
2018-06-07T18:17:55Z
dc.date.issued
2002-05
dc.identifier.citation
Sundberg, Eric J.; Li, Hongmin; Llera, Andrea Sabina; McCormick, John K.; Tormo, José; et al.; Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes; Cell Press; Structure With Folding & Design.; 10; 5; 5-2002; 687-699
dc.identifier.issn
0969-2126
dc.identifier.uri
http://hdl.handle.net/11336/47707
dc.description.abstract
Superantigens (SAGs) crosslink MHC class II and TCR molecules, resulting in an overstimulation of T cells associated with human disease. SAGs interact with several different surfaces on MHC molecules, necessitating the formation of multiple distinct MHC-SAG-TCR ternary signaling complexes. Variability in SAG-TCR binding modes could also contribute to the structural heterogeneity of SAG-dependent signaling complexes. We report crystal structures of the streptococcal SAGs SpeA and SpeC in complex with their corresponding TCR beta chain ligands that reveal distinct TCR binding modes. The SpeC-TCR beta chain complex structure, coupled with the recently determined SpeC-HLA-DR2a complex structure, provides a model for a novel T cell signaling complex that precludes direct TCR-MHC interactions. Thus, highly efficient T cell activation may be achieved through structurally diverse strategies of TCR ligation.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Cell Press
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Superantigen
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T Cell Receptor
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Structures of Two Streptococcal Superantigens Bound to TCR β Chains Reveal Diversity in the Architecture of T Cell Signaling Complexes
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-05-10T15:45:39Z
dc.identifier.eissn
1878-4186
dc.journal.volume
10
dc.journal.number
5
dc.journal.pagination
687-699
dc.journal.pais
Estados Unidos
dc.journal.ciudad
United States
dc.description.fil
Fil: Sundberg, Eric J.. University of Maryland; Estados Unidos
dc.description.fil
Fil: Li, Hongmin. University of Maryland; Estados Unidos
dc.description.fil
Fil: Llera, Andrea Sabina. University of Maryland; Estados Unidos. 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
dc.description.fil
Fil: McCormick, John K.. University of Minnesota; Estados Unidos
dc.description.fil
Fil: Tormo, José. University of Maryland; Estados Unidos. Universidad Autónoma de Madrid; España
dc.description.fil
Fil: Schlievert, Patrick M.. University of Minnesota; Estados Unidos
dc.description.fil
Fil: Karjalainen, Klaus. Basel Institute for Immunology; Suiza
dc.description.fil
Fil: Mariuzza, Roy A.. University of Maryland; Estados Unidos
dc.journal.title
Structure With Folding & Design.
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://linkinghub.elsevier.com/retrieve/pii/S0969212602007591
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1016/S0969-2126(02)00759-1
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