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Title
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Crystal structure of the MHC class I homolog MIC-A, a gammadelta T cell ligand.
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Authors
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P.Li,
S.T.Willie,
S.Bauer,
D.L.Morris,
T.Spies,
R.K.Strong.
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Ref.
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Immunity, 1999,
10,
577-584.
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PubMed id
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Abstract
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The major histocompatibility complex (MHC) class I homolog MIC-A functions as a
stress-inducible antigen that is recognized by a subset of gammadelta T cells
independent of beta2-microglobulin and bound peptides. Its crystal structure
reveals a dramatically altered MHC class I fold, both in detail and overall
domain organization. The only remnant of a peptide-binding groove is a small
cavity formed as the result of disordering a large section of one of the
groove-defining helices. Loss of beta2-microglobulin binding is due to a
restructuring of the interaction interfaces. Structural mapping of sequence
variation suggests potential receptor binding sites on the underside of the
platform on the side opposite of the surface recognized by alphabeta T cell
receptors on MHC class I-peptide complexes.
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