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The Journal of Immunology, 1999, 162: 846-851.
Copyright © 1999 by The American Association of Immunologists

Orientation of the Ig Domains of CD8{alpha}ß Relative to MHC Class I1

Lesley Devine*, Jiaren Sun*, Mark R. Barr* and Paula B. Kavathas2,*,{dagger}

* Department of Laboratory Medicine and Section of Immunobiology, and {dagger} Department of Genetics, Yale University School of Medicine, New Haven, CT 06520

The cell surface glycoprotein CD8 functions as a coreceptor with the TCR for interaction with MHC class I. The cocrystal structure of the CD8{alpha}{alpha}-MHC complex showed that one CD8 Ig domain provided the majority of the contact with MHC class I and that residue R4 of that domain contacted the {alpha}2 domain of MHC class I. We previously showed by mutational analysis that this residue was critical for binding to MHC class I. To determine which of the Ig domains for the CD8{alpha}ß heterodimer would make the most contact with class I MHC, we expressed single-chain or dimeric forms of CD8 on COS-7 cells and measured the adhesion of MHC class I positive cells. We found that when one of the R4 residues was mutated in a CD8{alpha}{alpha} homodimer binding comparable to that of wild type was observed, whereas a double R4 mutant severely impaired binding. However, when mutant CD8{alpha} (R4K) was coexpressed with wild-type CD8ß, binding was not observed. These results support the model in which it is CD8{alpha}, not CD8ß, that is making the most of the contact with MHC class I, including the {alpha}2 domain. In addition, they demonstrate that a single-chain form of CD8{alpha}{alpha} can bind to MHC class I.




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