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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| Publié dans: | Proc Natl Acad Sci U S A |
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| Auteurs principaux: | , , |
| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
National Academy of Sciences
1986
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| Sujets: | |
| Accès en ligne: | 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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