1BQH

MURINE CD8AA ECTODOMAIN FRAGMENT IN COMPLEX WITH H-2KB/VSV8

Summary for 1BQH

• Entry DOI: 10.2210/pdb1bqh/pdb
• Descriptor: PROTEIN (H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN), PROTEIN (BETA-2-MICROGLOBULIN ), PROTEIN (VSV8), ... (5 entities in total)
• Functional Keywords: t-cell, coreceptor, glycoprotein, complex, immunology, antigen, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 10
• Total formula weight: 147552.90

Authors

Wang, J.H.,Reinherz, E.L.,Kern, P.S.,Chang, H.C. (deposition date: 1998-08-16, release date: 1998-08-19, Last modification date: 2024-10-30)

Primary citation

Kern, P.S.,Teng, M.K.,Smolyar, A.,Liu, J.H.,Liu, J.,Hussey, R.E.,Spoerl, R.,Chang, H.C.,Reinherz, E.L.,Wang, J.H.
Structural basis of CD8 coreceptor function revealed by crystallographic analysis of a murine CD8alphaalpha ectodomain fragment in complex with H-2Kb.
Immunity, 9:519-530, 1998

PubMed Abstract: 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.

PubMed: 9806638
DOI: 10.1016/S1074-7613(00)80635-4

Experimental method

X-RAY DIFFRACTION (2.8 Å)