1hqr

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[[Image:1hqr.gif|left|200px]]
[[Image:1hqr.gif|left|200px]]
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{{Structure
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|PDB= 1hqr |SIZE=350|CAPTION= <scene name='initialview01'>1hqr</scene>, resolution 3.20&Aring;
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The line below this paragraph, containing "STRUCTURE_1hqr", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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{{STRUCTURE_1hqr| PDB=1hqr | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hqr OCA], [http://www.ebi.ac.uk/pdbsum/1hqr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hqr RCSB]</span>
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'''CRYSTAL STRUCTURE OF A SUPERANTIGEN BOUND TO THE HIGH-AFFINITY, ZINC-DEPENDENT SITE ON MHC CLASS II'''
'''CRYSTAL STRUCTURE OF A SUPERANTIGEN BOUND TO THE HIGH-AFFINITY, ZINC-DEPENDENT SITE ON MHC CLASS II'''
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[[Category: Mariuzza, R.]]
[[Category: Mariuzza, R.]]
[[Category: Schlievert, P.]]
[[Category: Schlievert, P.]]
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[[Category: superantigen-mhc class ii complex]]
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[[Category: Superantigen-mhc class ii complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:08:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:09:10 2008''
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Revision as of 16:08, 2 May 2008

Template:STRUCTURE 1hqr

CRYSTAL STRUCTURE OF A SUPERANTIGEN BOUND TO THE HIGH-AFFINITY, ZINC-DEPENDENT SITE ON MHC CLASS II


Overview

MHC class II molecules possess two binding sites for bacterial superantigens (SAGs): a low-affinity site on the alpha chain and a high-affinity, zinc-dependent site on the beta chain. Only the former has been defined crystallographically. We report the structure of streptococcal pyrogenic exotoxin C (SPE-C) complexed with HLA-DR2a (DRA*0101, DRB5*0101) bearing a self-peptide from myelin basic protein (MBP). SPE-C binds the beta chain through a zinc bridge that links the SAG and class II molecules. Surprisingly, SPE-C also makes extensive contacts with the MBP peptide, such that peptide accounts for one third of the surface area of the MHC molecule buried in the complex, similar to TCR-peptide/MHC complexes. Thus, SPE-C may optimize T cell responses by mimicking the peptide dependence of conventional antigen presentation and recognition.

About this Structure

1HQR is a Protein complex structure of sequences from Homo sapiens and Streptococcus pyogenes. Full crystallographic information is available from OCA.

Reference

Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on MHC class II., Li Y, Li H, Dimasi N, McCormick JK, Martin R, Schuck P, Schlievert PM, Mariuzza RA, Immunity. 2001 Jan;14(1):93-104. PMID:11163233 Page seeded by OCA on Fri May 2 19:08:11 2008

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