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. 1993 Jul 1;364(6432):33-9.
doi: 10.1038/364033a0.

Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1

J H Brown  1 , T S Jardetzky, J C Gorga, L J Stern, R G Urban, J L Strominger, D C Wiley
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Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1

J H Brown et al. Nature. .

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.

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