1ktk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1ktk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ktk, resolution 3.00&Aring;" /> '''Complex of Streptoc...)
Line 1: Line 1:
-
[[Image:1ktk.gif|left|200px]]<br />
+
[[Image:1ktk.gif|left|200px]]<br /><applet load="1ktk" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1ktk" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1ktk, resolution 3.00&Aring;" />
caption="1ktk, resolution 3.00&Aring;" />
'''Complex of Streptococcal pyrogenic enterotoxin C (SpeC) with a human T cell receptor beta chain (Vbeta2.1)'''<br />
'''Complex of Streptococcal pyrogenic enterotoxin C (SpeC) with a human T cell receptor beta chain (Vbeta2.1)'''<br />
==Overview==
==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.
+
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==
-
1KTK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KTK OCA].
+
1KTK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KTK OCA].
==Reference==
==Reference==
Line 17: Line 16:
[[Category: Karjalainen, K.]]
[[Category: Karjalainen, K.]]
[[Category: Li, H.]]
[[Category: Li, H.]]
-
[[Category: Llera, A.S.]]
+
[[Category: Llera, A S.]]
-
[[Category: Mariuzza, R.A.]]
+
[[Category: Mariuzza, R A.]]
-
[[Category: McCormick, J.K.]]
+
[[Category: McCormick, J K.]]
-
[[Category: Schlievert, P.M.]]
+
[[Category: Schlievert, P M.]]
-
[[Category: Sundberg, E.J.]]
+
[[Category: Sundberg, E J.]]
[[Category: Tormo, J.]]
[[Category: Tormo, J.]]
[[Category: immunity]]
[[Category: immunity]]
Line 27: Line 26:
[[Category: t cell receptor beta]]
[[Category: t cell receptor beta]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:54:34 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:50 2008''

Revision as of 11:37, 21 February 2008


1ktk, resolution 3.00Å

Drag the structure with the mouse to rotate

Complex of Streptococcal pyrogenic enterotoxin C (SpeC) with a human T cell receptor beta chain (Vbeta2.1)

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

1KTK is a Protein complex structure of sequences from Homo sapiens 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 Thu Feb 21 13:37:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools