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Title
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Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1.
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Authors
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J.H.Brown,
T.S.Jardetzky,
J.C.Gorga,
L.J.Stern,
R.G.Urban,
J.L.Strominger,
D.C.Wiley.
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Ref.
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Nature, 1993,
364,
33-39.
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PubMed id
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Abstract
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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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