doi: 10.1038/364033a0.
Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1
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- PMID: 8316295
- DOI: 10.1038/364033a0
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Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1
Nature.
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Abstract
The three-dimensional structure of the class II histocompatibility glycoprotein HLA-DR1 from human B-cell membranes has been determined by X-ray crystallography and is similar to that of class I HLA. Peptides are bound in an extended conformation that projects from both ends of an 'open-ended' antigen-binding groove. A prominent non-polar pocket into which an 'anchoring' peptide side chain fits is near one end of the binding groove. A dimer of the class II alpha beta heterodimers is seen in the crystal forms of HLA-DR1, suggesting class II HLA dimerization as a mechanism for initiating the cytoplasmic signalling events in T-cell activation.
Comment in
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Immunology. MHC class II dimer of dimers.Nature. 1993 Jul 1;364(6432):16-7. doi: 10.1038/364016d0. Nature. 1993. PMID: 8316292 No abstract available.
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Pillars article: three-dimensional structure of the human class II histocompatibility antigen HLA-DR1. Nature. 1993. 364: 33-39.J Immunol. 2015 Jan 1;194(1):5-11. J Immunol. 2015. PMID: 25527791 No abstract available.
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