| First Author | Kern PS | Year | 1998 |
| Journal | Immunity | Volume | 9 |
| Issue | 4 | Pages | 519-30 |
| PubMed ID | 9806638 | Mgi Jnum | J:50625 |
| Mgi Id | MGI:1307020 | Doi | 10.1016/s1074-7613(00)80635-4 |
| Citation | Kern PS, et al. (1998) Structural basis of CD8 coreceptor function revealed by crystallographic analysis of a murine CD8alphaalpha ectodomain fragment in complex with H-2Kb. Immunity 9(4):519-30 |
| abstractText | The crystal structure of the two immunoglobulin variable-like domains of the murine CD8alphaalpha homodimer complexed to the class I MHC H-2Kb molecule at 2.8 A resolution shows that CD8alphaalpha binds to the protruding MHC alpha3 domain loop in an antibody-like manner. Comparison of mouse CD8alphaalpha/H-2Kb and human CD8alphaalpha/HLA-A2 complexes reveals shared as well as species-specific recognition features. In both species, coreceptor function apparently involves the participation of CD8 dimer in a bidentate attachment to an MHC class I molecule in conjunction with a T cell receptor without discernable conformational alteration of the peptide or MHC antigen-presenting platform. |
