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The Journal of Immunology, Vol 151, Issue 11 6089-6098, Copyright © 1993 by American Association of Immunologists
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DJ Connolly, LA Cotterill, RA Hederer, CJ Thorpe, PJ Travers, JH McVey, J Dyson and PJ Robinson
Transplantation Biology Section, Clinical Research Centre, Harrow, UK.
We have isolated a cDNA clone which encodes the Qa-1a histocompatibility Ag from a library prepared from Con A-activated B10.BR mouse spleen cells. The clone encodes a protein of 322 amino acids with three potential N-glycosylation sites. The coding sequence shows strongest similarity with that of the T23d gene of DBA/2 mice which encodes the Qa-1b molecule. Molecular modeling of the putative peptide-combining site indicates most of the differences between Qa-1a and Qa-1b are located peripheral to the binding cleft, with only two amino acid substitutions, at positions 9 and 24, which might affect peptide binding. Many features of the Qa-1 binding cleft are also conserved in the rat RTBM.1 and in human HLA-E molecules. This suggests that all of these molecules may associate with structurally similar peptides.
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