2ntt
From Proteopedia
(New page: 200px<br /><applet load="2ntt" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ntt, resolution 1.561Å" /> '''Crystal Structure o...) |
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==Overview== | ==Overview== | ||
| - | Superantigens (SAGs) interact with host immune receptors to induce a | + | Superantigens (SAGs) interact with host immune receptors to induce a massive release of inflammatory cytokines that can lead to toxic shock syndrome and death. Bacterial SAGs can be classified into five distinct evolutionary groups. Group V SAGs are characterized by the alpha3-beta8 loop, a unique approximately 15 amino acid residue extension that is required for optimal T cell activation. Here, we report the X-ray crystal structures of the group V SAG staphylococcal enterotoxin K (SEK) alone and in complex with the TCR hVbeta5.1 domain. SEK adopts a unique TCR binding orientation relative to other SAG-TCR complexes, which results in the alpha3-beta8 loop contacting the apical loop of framework region 4, thereby extending the known TCR recognition site of SAGs. These interactions are absolutely required for TCR binding and T cell activation by SEK, and dictate the TCR Vbeta domain specificity of SEK and other group V SAGs. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | A | + | A novel loop domain in superantigens extends their T cell receptor recognition site., Gunther S, Varma AK, Moza B, Kasper KJ, Wyatt AW, Zhu P, Rahman AK, Li Y, Mariuzza RA, McCormick JK, Sundberg EJ, J Mol Biol. 2007 Aug 3;371(1):210-21. Epub 2007 May 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17560605 17560605] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Gunther, S.]] | [[Category: Gunther, S.]] | ||
[[Category: Moza, B.]] | [[Category: Moza, B.]] | ||
| - | [[Category: Sundberg, E | + | [[Category: Sundberg, E J.]] |
| - | [[Category: Varma, A | + | [[Category: Varma, A K.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: superantigen; t cell receptor]] | [[Category: superantigen; t cell receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:56 2008'' |
Revision as of 16:10, 21 February 2008
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Crystal Structure of SEK
Overview
Superantigens (SAGs) interact with host immune receptors to induce a massive release of inflammatory cytokines that can lead to toxic shock syndrome and death. Bacterial SAGs can be classified into five distinct evolutionary groups. Group V SAGs are characterized by the alpha3-beta8 loop, a unique approximately 15 amino acid residue extension that is required for optimal T cell activation. Here, we report the X-ray crystal structures of the group V SAG staphylococcal enterotoxin K (SEK) alone and in complex with the TCR hVbeta5.1 domain. SEK adopts a unique TCR binding orientation relative to other SAG-TCR complexes, which results in the alpha3-beta8 loop contacting the apical loop of framework region 4, thereby extending the known TCR recognition site of SAGs. These interactions are absolutely required for TCR binding and T cell activation by SEK, and dictate the TCR Vbeta domain specificity of SEK and other group V SAGs.
About this Structure
2NTT is a Single protein structure of sequence from Staphylococcus aureus with and as ligands. Full crystallographic information is available from OCA.
Reference
A novel loop domain in superantigens extends their T cell receptor recognition site., Gunther S, Varma AK, Moza B, Kasper KJ, Wyatt AW, Zhu P, Rahman AK, Li Y, Mariuzza RA, McCormick JK, Sundberg EJ, J Mol Biol. 2007 Aug 3;371(1):210-21. Epub 2007 May 18. PMID:17560605
Page seeded by OCA on Thu Feb 21 18:10:56 2008
