Journal article
Crystal Structure of a Superantigen Bound to the High-Affinity, Zinc-Dependent Site on MHC Class II
Immunity (Cambridge, Mass.), Vol.14(1), pp.93-104
2001
DOI: 10.1016/S1074-7613(01)00092-9
PMID: 11163233
Abstract
MHC class II molecules possess two binding sites for bacterial superantigens (SAGs): a low-affinity site on the α chain and a high-affinity, zinc-dependent site on the β 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 β 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.
Details
- Title: Subtitle
- Crystal Structure of a Superantigen Bound to the High-Affinity, Zinc-Dependent Site on MHC Class II
- Creators
- Yili Li - Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850, USAHongmin Li - Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850, USANazzareno Dimasi - Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850, USAJohn K McCormick - Department of Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota 55455, USARoland Martin - Neuroimmunology Branch, National Institute of Neurological, Disorders and Stroke, Bethesda, Maryland 20892, USAPeter Schuck - Molecular Interactions Resource, Division of Bioengineering and Physical Sciences, National Institutes of Health, Bethesda, Maryland 20892, USAPatrick M Schlievert - Department of Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota 55455, USARoy A Mariuzza - Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850, USA
- Resource Type
- Journal article
- Publication Details
- Immunity (Cambridge, Mass.), Vol.14(1), pp.93-104
- Publisher
- Elsevier Inc
- DOI
- 10.1016/S1074-7613(01)00092-9
- PMID
- 11163233
- ISSN
- 1074-7613
- eISSN
- 1097-4180
- Language
- English
- Date published
- 2001
- Academic Unit
- Microbiology and Immunology; Internal Medicine
- Record Identifier
- 9984001159902771
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