A novel MHC-I surface targeted for binding by the MCMV m06 immunoevasin revealed by solution NMR

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Abstract

Background: The m06/gp48 protein of MCMV binds to MHC-I proteins, diverting them to lysosomes. Results: Recombinant m06 binds weakly to H2-Ld MHC-I and tightly to mini-H2-Ld, which provides excellent NMR spectra for mapping the binding site. Conclusion: The binding site on MHC-I partially overlaps with the β2m interface. Significance: Thus, m06 may alter the conformation of β2m association with MHC-I heavy chain following m06 binding in a viral infection.

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Sgourakis, N. G., May, N. A., Boyd, L. F., Ying, J., Bax, A., & Margulies, D. H. (2015). A novel MHC-I surface targeted for binding by the MCMV m06 immunoevasin revealed by solution NMR. Journal of Biological Chemistry, 290(48), 28857–28868. https://doi.org/10.1074/jbc.M115.689661

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