Crystal structure of the complex between human CD8alpha(alpha) and HLA-A2.
The dimeric cell-surface glycoprotein CD8 is crucial to the positive selection of cytotoxic T cells in the thymus. The homodimer CD8alpha(alpha) or the heterodimer alpha beta stabilizes the interaction of the T-cell antigen receptor (TCR) with major histocompatibility complex (MHC) class I/peptide b...
Váldodahkkit: | Gao, G, Tormo, J, Gerth, U, Wyer, JR, McMichael, A, Stuart, D, Bell, J, Jones, E, Jakobsen, B |
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Materiálatiipa: | Journal article |
Giella: | English |
Almmustuhtton: |
1997
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Geahča maid
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Crystal structure of the complex between CD8αα human and HLA-A2
Dahkki: Gao, G, et al.
Almmustuhtton: (1997) -
Assembly and crystallization of the complex between the human T cell coreceptor CD8alpha homodimer and HLA-A2.
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An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501.
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T cell receptor and coreceptor CD8 alphaalpha bind peptide-MHC independently and with distinct kinetics.
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Almmustuhtton: (1999) -
Production, crystallization, and preliminary X-ray analysis of the human MHC class Ib molecule HLA-E.
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Almmustuhtton: (1998)