Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1
JH Brown, TS Jardetzky, JC Gorga, LJ Stern, RG Urban… - Nature, 1993 - nature.com
JH Brown, TS Jardetzky, JC Gorga, LJ Stern, RG Urban, JL Strominger, DC Wiley
Nature, 1993•nature.comThe 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 αβ heterodimers is seen in the crystal forms of HLA-DR1, suggesting class II HLA …
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 αβ heterodimers is seen in the crystal forms of HLA-DR1, suggesting class II HLA …
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 αβ 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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