2ATP

Crystal structure of a CD8ab heterodimer

Summary for 2ATP

• Entry DOI: 10.2210/pdb2atp/pdb
• Related: 1BQH 1NEZ
• Descriptor: T-cell surface glycoprotein CD8 alpha chain, artifact linker, T-cell surface glycoprotein CD8 beta chain, ... (5 entities in total)
• Functional Keywords: cd8ab, cd8aa, mhc, immune system
• Biological source: Mus musculus (house mouse); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01731 P10300
• Total number of polymer chains: 6
• Total formula weight: 60483.72

Authors

Chang, H.C.,Tan, K.,Ouyang, J.,Parisini, E.,Liu, J.H.,Le, Y.,Wang, X.,Reinherz, E.L.,Wang, J.H. (deposition date: 2005-08-25, release date: 2005-12-27, Last modification date: 2024-10-30)

Primary citation

Chang, H.C.,Tan, K.,Ouyang, J.,Parisini, E.,Liu, J.H.,Le, Y.,Wang, X.,Reinherz, E.L.,Wang, J.H.
Structural and Mutational Analyses of a CD8alphabeta Heterodimer and Comparison with the CD8alphaalpha Homodimer.
Immunity, 23:661-671, 2005

PubMed Abstract: The crystal structure of a recombinant mouse single chain CD8alphabeta ectodomains at 2.4 A resolution reveals paired immunoglobulin variable region-like domains with a striking resemblance to CD8alphaalpha in size, shape, and surface electrostatic potential of complementarity-determining regions (CDR), despite <20% sequence identity between the CD8alpha and CD8beta subunits. Unlike the CD8alpha subunit(s) in the heterodimer or homodimer, the CDR1 loop of CD8beta tilts away from its corresponding CDR2 and CDR3 loops. Consistent with this observation, independent mutational studies reveal that alanine substitutions of residues in the CDR1 loop of CD8beta have no effect on CD8alphabeta coreceptor function, whereas mutations in CD8beta CDR2 and CDR3 loops abolish CD8alphabeta coreceptor activity. The implications of these findings and additional CD8alpha mutational studies for CD8alphabeta- versus CD8alphaalpha-MHCI binding are discussed.

PubMed: 16356863
DOI: 10.1016/j.immuni.2005.11.002

Experimental method

X-RAY DIFFRACTION (2.4 Å)