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The solvent-inaccessible Cys67 residue of HLA-B27 contributes to T cell recognition of HLA-B27/peptide complexes.

Abstract:

Crystallographic studies have suggested that the cysteine at position 67 (Cys(67)) in the B pocket of the MHC molecule HLA-B*2705 is of importance for peptide binding, and biophysical studies have documented altered thermodynamic stability of the molecule when Cys(67) was mutated to serine (Ser(67)). In this study, we used HLA-B27.Cys(67) and HLA-B27.Ser(67) tetramers with defined T cell epitopes to determine the contribution of this polymorphic, solvent-inaccessible MHC residue to T cell rec...

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Publication status:
Published

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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
NDM Experimental Medicine
Role:
Author
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Journal:
Journal of Immunology
Volume:
173
Issue:
11
Pages:
6564-6573
Publication date:
2004-12-01
DOI:
EISSN:
1550-6606
ISSN:
0022-1767
Source identifiers:
32918

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