1l0x
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| - | |DOMAIN= | + | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00098 IGc], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd00099 IGv], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam07686 V-set], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam02876 Stap_Strp_tox_C], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam01123 Stap_Strp_toxin]</span> |
|RELATEDENTRY=[[1sbb|1SBB]], [[1jck|1JCK]], [[1l0y|1L0Y]] | |RELATEDENTRY=[[1sbb|1SBB]], [[1jck|1JCK]], [[1l0y|1L0Y]] | ||
| - | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l0x OCA], [http://www.ebi.ac.uk/pdbsum/1l0x PDBsum | + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l0x OCA], [http://www.ebi.ac.uk/pdbsum/1l0x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l0x RCSB]</span> |
}} | }} | ||
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[[Category: tcr]] | [[Category: tcr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:56:26 2008'' |
Revision as of 18:56, 30 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Domains: | IGc, IGv, V-set, Stap_Strp_tox_C, Stap_Strp_toxin | ||||||
| Related: | 1SBB, 1JCK, 1L0Y
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
TCR beta chain complexed with streptococcal superantigen SpeA
Overview
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.
About this Structure
1L0X is a Protein complex structure of sequences from Mus musculus and Streptococcus pyogenes. Full crystallographic information is available from OCA.
Reference
Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes., Sundberg EJ, Li H, Llera AS, McCormick JK, Tormo J, Schlievert PM, Karjalainen K, Mariuzza RA, Structure. 2002 May;10(5):687-99. PMID:12015151
Page seeded by OCA on Sun Mar 30 21:56:26 2008
