1hxy

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(New page: 200px<br /> <applet load="1hxy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hxy, resolution 2.6&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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<applet load="1hxy" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1hxy, resolution 2.6&Aring;" />
'''CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN H IN COMPLEX WITH HUMAN MHC CLASS II'''<br />
'''CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN H IN COMPLEX WITH HUMAN MHC CLASS II'''<br />
==Overview==
==Overview==
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The three-dimensional structure of a bacterial superantigen, Staphylococcus aureus enterotoxin H (SEH), bound to human major, histocompatibility complex (MHC) class II (HLA-DR1) has been determined by, X-ray crystallography to 2.6 A resolution (1HXY). The superantigen binds, on top of HLA-DR1 in a completely different way from earlier, co-crystallized superantigens from S.aureus. SEH interacts with high, affinity through a zinc ion with the beta1 chain of HLA-DR1 and also with, the peptide presented by HLA-DR1. The structure suggests that all, superantigens interacting with MHC class II in a zinc-dependent manner, present the superantigen in a common way. This suggests a new model for, ternary complex formation with the T-cell receptor (TCR), in which a, contact between the TCR and the MHC class II is unlikely.
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The three-dimensional structure of a bacterial superantigen, Staphylococcus aureus enterotoxin H (SEH), bound to human major histocompatibility complex (MHC) class II (HLA-DR1) has been determined by X-ray crystallography to 2.6 A resolution (1HXY). The superantigen binds on top of HLA-DR1 in a completely different way from earlier co-crystallized superantigens from S.aureus. SEH interacts with high affinity through a zinc ion with the beta1 chain of HLA-DR1 and also with the peptide presented by HLA-DR1. The structure suggests that all superantigens interacting with MHC class II in a zinc-dependent manner present the superantigen in a common way. This suggests a new model for ternary complex formation with the T-cell receptor (TCR), in which a contact between the TCR and the MHC class II is unlikely.
==About this Structure==
==About this Structure==
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1HXY 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/Staphylococcus_aureus Staphylococcus aureus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HXY OCA].
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1HXY 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/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HXY OCA].
==Reference==
==Reference==
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[[Category: Nilsson, H.]]
[[Category: Nilsson, H.]]
[[Category: Petersson, K.]]
[[Category: Petersson, K.]]
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[[Category: Svensson, L.A.]]
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[[Category: Svensson, L A.]]
[[Category: Walse, B.]]
[[Category: Walse, B.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: complex]]
[[Category: complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:24:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:56 2008''

Revision as of 11:05, 21 February 2008


1hxy, resolution 2.6Å

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CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN H IN COMPLEX WITH HUMAN MHC CLASS II

Overview

The three-dimensional structure of a bacterial superantigen, Staphylococcus aureus enterotoxin H (SEH), bound to human major histocompatibility complex (MHC) class II (HLA-DR1) has been determined by X-ray crystallography to 2.6 A resolution (1HXY). The superantigen binds on top of HLA-DR1 in a completely different way from earlier co-crystallized superantigens from S.aureus. SEH interacts with high affinity through a zinc ion with the beta1 chain of HLA-DR1 and also with the peptide presented by HLA-DR1. The structure suggests that all superantigens interacting with MHC class II in a zinc-dependent manner present the superantigen in a common way. This suggests a new model for ternary complex formation with the T-cell receptor (TCR), in which a contact between the TCR and the MHC class II is unlikely.

About this Structure

1HXY is a Protein complex structure of sequences from Homo sapiens and Staphylococcus aureus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence., Petersson K, Hakansson M, Nilsson H, Forsberg G, Svensson LA, Liljas A, Walse B, EMBO J. 2001 Jul 2;20(13):3306-12. PMID:11432818

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