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PDBsum entry 3bdw
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Immune system receptor
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PDB id
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3bdw
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References listed in PDB file
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Key reference
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Title
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The heterodimeric assembly of the cd94-Nkg2 receptor family and implications for human leukocyte antigen-E recognition.
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Authors
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L.C.Sullivan,
C.S.Clements,
T.Beddoe,
D.Johnson,
H.L.Hoare,
J.Lin,
T.Huyton,
E.J.Hopkins,
H.H.Reid,
M.C.Wilce,
J.Kabat,
F.Borrego,
J.E.Coligan,
J.Rossjohn,
A.G.Brooks.
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Ref.
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Immunity, 2007,
27,
900-911.
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PubMed id
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Abstract
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The CD94-NKG2 receptor family that regulates NK and T cells is unique among the
lectin-like receptors encoded within the natural killer cell complex. The
function of the CD94-NKG2 receptors is dictated by the pairing of the invariant
CD94 polypeptide with specific NKG2 isoforms to form a family of functionally
distinct heterodimeric receptors. However, the structural basis for this
selective pairing and how they interact with their ligand, HLA-E, is unknown. We
describe the 2.5 A resolution crystal structure of CD94-NKG2A in which the mode
of dimerization contrasts with that of other homodimeric NK receptors. Despite
structural homology between the CD94 and NKG2A subunits, the dimer interface is
asymmetric, thereby providing a structural basis for the preferred heterodimeric
assembly. Structure-based sequence comparisons of other CD94-NKG2 family
members, combined with extensive mutagenesis studies on HLA-E and CD94-NKG2A,
allows a model of the interaction between CD94-NKG2A and HLA-E to be
established, in which the invariant CD94 chain plays a more dominant role in
interacting with HLA-E in comparison to the variable NKG2 chain.
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