Journal article
A structural basis for antigen presentation by the MHC class Ib molecule, Qa-1 b
L Zeng, LC Sullivan, JP Vivian, NG Walpole, CM Harpur, J Rossjohn, CS Clements, AG Brooks
Journal of Immunology | AMER ASSOC IMMUNOLOGISTS | Published : 2012
Abstract
The primary function of the monomorphic MHC class Ib molecule Qa-1 b is to present peptides derived from the leader sequences of other MHC class I molecules for recognition by the CD94-NKG2 receptors expressed by NK and T cells. Whereas the mode of peptide presentation by its ortholog HLA-E, and subsequent recognition by CD94-NKG2A, is known, the molecular basis of Qa-1 bfunction is unclear. We have assessed the interaction between Qa-1 b and CD94-NKG2A and shown that they interact with an affinity of 17 μM. Furthermore, we have determined the structure of Qa-1 b bound to the leader sequence peptide, Qdm (AMAPRTLLL), to a resolution of 1.9 Å and compared it with that of HLA-E. The crystal st..
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Funding Acknowledgements
This work was supported by grants from the Australian Research Council and the National Health and Medical Research Council; an Australian postgraduate scholarship (to L.Z.); a Career Development award from the National Health and Medical Research Council (to L. C. S.); a Doherty fellowship from the National Health and Medical Research Council (to J.P.V.); a Federation fellowship from the Australian Research Council (to J.R.); and a Queen Elizabeth II fellowship from the Australian Research Council (to C.S.C.).