A binding site for the T-cell co-receptor CD8 on the α3 domain of HLA-A2
RD Salter, RJ Benjamin, PK Wesley, SE Buxton… - Nature, 1990 - nature.com
RD Salter, RJ Benjamin, PK Wesley, SE Buxton, TPJ Garrett, C Clayberger, AM Krensky…
Nature, 1990•nature.comAdhesion measurements between CD8 and 48 point mutants of HLA-A2. 1 show that the
CD8 α-chain binds to the α3 domain of HLA-A2. 1. Three clusters of α3 residues contribute
to the binding, with an exposed, negatively charged loop (residues 223–229) playing a
dominant role. CD8 binding correlates with cytotoxic T-cell recognition and sensitivity to
inhibition by anti-CD8 antibodies. Impaired alloreactive T-cell recognition of an HLA-A2. 1
mutant with reduced affinity for CD8 is not restored by functional CD8 binding sites on an …
CD8 α-chain binds to the α3 domain of HLA-A2. 1. Three clusters of α3 residues contribute
to the binding, with an exposed, negatively charged loop (residues 223–229) playing a
dominant role. CD8 binding correlates with cytotoxic T-cell recognition and sensitivity to
inhibition by anti-CD8 antibodies. Impaired alloreactive T-cell recognition of an HLA-A2. 1
mutant with reduced affinity for CD8 is not restored by functional CD8 binding sites on an …
Abstract
Adhesion measurements between CD8 and 48 point mutants of HLA-A2.1 show that the CD8 α-chain binds to the α3 domain of HLA-A2.1. Three clusters of α3 residues contribute to the binding, with an exposed, negatively charged loop (residues 223–229) playing a dominant role. CD8 binding correlates with cytotoxic T-cell recognition and sensitivity to inhibition by anti-CD8 antibodies. Impaired alloreactive T-cell recognition of an HLA-A2.1 mutant with reduced affinity for CD8 is not restored by functional CD8 binding sites on an antigenically irrelevant class I molecule. Therefore, complexes of CD8 and the T-cell receptor bound to the same class I major histocompatibility complex molecule seem to be necessary for T-cell activation.
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