Journal of Molecular Biology
CommunicationSubtle Changes in Peptide Conformation Profoundly Affect Recognition of the Non-Classical MHC Class I Molecule HLA-E by the CD94–NKG2 Natural Killer Cell Receptors
Section snippets
Structural determination and analysis of HLA-E/peptide complexes
Previous studies have shown that substitutions at P6 and P8 of the HLA-E peptide have a direct effect on the affinity of the interaction between CD94–NKG2A and HLA-E.15, 17, 18 To better understand the structural basis for the observed peptide-dependent differences in the affinity of CD94–NKG2 receptors for HLA-E, we determined the crystal structure of HLA-E in complex with the HLA-G*01 leader sequence peptide (VMAPRTLFL, HLA-EVMAPRTLFL), which interacted with the CD94–NKG2 receptors with the
Acknowledgements
The National Health and Medical Research Council (NHMRC) and the Australian Research Council (ARC) supported this work. L.S. and T.B. are supported by a Peter Doherty NHMRC Fellowship and NHMRC and Career Development Award, respectively. C.S.C. is supported by an ARC Queen Elizabeth II Fellowship, and J.R. is supported by an ARC Federation Fellowship. We thank the staff at BioCars for their assistance with data collection.
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Cited by (0)
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H.L.H. and L.C.S. contributed equally to this work.
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A.G.B. and J.R. are the senior authors of this work.