1hqr: Difference between revisions

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|PDB= 1hqr |SIZE=350|CAPTION= <scene name='initialview01'>1hqr</scene>, resolution 3.20&Aring;
|PDB= 1hqr |SIZE=350|CAPTION= <scene name='initialview01'>1hqr</scene>, resolution 3.20&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|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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==Overview==
==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.
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.
==Disease==
Known diseases associated with this structure: Chronic infections, due to MBL deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=154545 154545]], Diabetes mellitus, gestational, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=154545 154545]], Mannose-binding protein deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=154545 154545]], Meningococcal disease, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=154545 154545]]


==About this Structure==
==About this Structure==
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[[Category: Mariuzza, R.]]
[[Category: Mariuzza, R.]]
[[Category: Schlievert, P.]]
[[Category: Schlievert, P.]]
[[Category: ZN]]
[[Category: superantigen-mhc class ii complex]]
[[Category: superantigen-mhc class ii complex]]


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