Structural basis of CD8 coreceptor function revealed by crystallographic analysis of a murine CD8αα ectodomain fragment in complex with H-2K

156Citations
Citations of this article
41Readers
Mendeley users who have this article in their library.

Abstract

The crystal structure of the two immunoglobulin variable-like domains of the murine CD8αα homodimer complexed to the class I MHC H-2Kb molecule at 2.8 Å resolution shows that CD8αα binds to the protruding MHC α3 domain loop in an antibody-like manner. Comparison of mouse CD8αα/H-2Kb and human CD8αα/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.

Cite

CITATION STYLE

APA

Kern, P. S., Teng, M. kun, Smolyar, A., Liu, J. huan, Liu, J., Hussey, R. E., … Wang, J. huai. (1998). Structural basis of CD8 coreceptor function revealed by crystallographic analysis of a murine CD8αα ectodomain fragment in complex with H-2K. Immunity, 9(4), 519–530. https://doi.org/10.1016/S1074-7613(00)80635-4

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free