2atp
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Crystal structure of a CD8ab heterodimer
OverviewOverview
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.
About this StructureAbout this Structure
2ATP is a Protein complex structure of sequences from Mus musculus with NAG as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Structural and mutational analyses of a CD8alphabeta heterodimer and comparison with the CD8alphaalpha homodimer., Chang HC, Tan K, Ouyang J, Parisini E, Liu JH, Le Y, Wang X, Reinherz EL, Wang JH, Immunity. 2005 Dec;23(6):661-71. PMID:16356863
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