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The isolated major histocompatibility complex class I alpha3 domain binds beta2m and CD8alphaalpha dimers.

M C Whitman·J Strohmaier·K O'Boyle·J M Tingem·Y Wilkinson·J Goldstein·T Chen·K Brorson·M Brunswick·S Kozlowski
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Abstract

The MHC class I molecule plays a crucial role in cytotoxic lymphocyte function. The heavy chain of the MHC class I molecule can form many non-covalent interactions with other molecules on multiple domains and surfaces. We have generated an isolated alpha3 domain of a murine MHC class I molecule and evaluated the contribution of this domain to binding with the MHC class I light chain, beta2m, and CD8. The alpha3 domain binds beta2m at a thousand-fold higher concentration than the whole MHC, and binds CD8alphaalpha with a dependence on the alpha3 CD loop. Our results are relevant for models of MHC folding and CD8-MHC function. The study of individual domains of complex molecules is an important strategy for understanding their dynamic structure and function.

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Binding SitesCD8 AntigensH-2 AntigensHistocompatibility Antigen H-2DMutationPeptide FragmentsProtein BindingProtein Structure, Tertiarybeta 2-MicroglobulinJournal Article

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BibTeXRIS

M C Whitman, J Strohmaier, K O'Boyle, J M Tingem, Y Wilkinson, J Goldstein, T Chen, K Brorson, M Brunswick, S Kozlowski. The isolated major histocompatibility complex class I alpha3 domain binds beta2m and CD8alphaalpha dimers.. https://doi.org/10.1016/s0161-5890(00)00034-1

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