The isolated major histocompatibility complex class I alpha3 domain binds beta2m and CD8alphaalpha dimers |
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Authors: | Whitman M C Strohmaier J O'Boyle K Tingem J M Wilkinson Y Goldstein J Chen T Brorson K Brunswick M Kozlowski S |
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Affiliation: | Division of Monoclonal Ab, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892, USA. |
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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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