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Intracellular transport blockade caused by disruption of the disulfide bridge in the third external domain of major histocompatibility complex class I antigen.

The third external domain of major histocompatibility class I antigens has a highly conserved disulfide bridge between cysteine-203 and cysteine-259. To elucidate the functional significance of this disulfide bridge, we have produced a mutant H-2Ld gene by site-directed mutagenesis in which the codo...

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Detalhes bibliográficos
Publicado no:Proc Natl Acad Sci U S A
Main Authors: Miyazaki, J, Appella, E, Ozato, K
Formato: Artigo
Idioma:Inglês
Publicado em: National Academy of Sciences 1986
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC322944/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3080749/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.83.3.757
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