1l0y

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(New page: 200px<br /><applet load="1l0y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l0y, resolution 2.5&Aring;" /> '''T cell receptor beta ...)
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[[Image:1l0y.gif|left|200px]]<br /><applet load="1l0y" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1l0y.gif|left|200px]]<br /><applet load="1l0y" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1l0y, resolution 2.5&Aring;" />
caption="1l0y, resolution 2.5&Aring;" />
'''T cell receptor beta chain complexed with superantigen SpeA soaked with zinc'''<br />
'''T cell receptor beta chain complexed with superantigen SpeA soaked with zinc'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1L0Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes] with ZN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L0Y OCA].
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1L0Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L0Y OCA].
==Reference==
==Reference==
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[[Category: Streptococcus pyogenes]]
[[Category: Streptococcus pyogenes]]
[[Category: Li, H.]]
[[Category: Li, H.]]
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[[Category: Mariuzza, R.A.]]
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[[Category: Mariuzza, R A.]]
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[[Category: Sundberg, E.J.]]
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[[Category: Sundberg, E J.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: tcr]]
[[Category: tcr]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:09:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:05 2008''

Revision as of 11:40, 21 February 2008

Image:1l0y.gif

1l0y, resolution 2.5Å

Drag the structure with the mouse to rotate

T cell receptor beta chain complexed with superantigen SpeA soaked with zinc

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

1L0Y is a Protein complex structure of sequences from Mus musculus and Streptococcus pyogenes with and as ligands. 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

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