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Peptide exchange on MHC-I by TAPBPR is driven by a negative allostery release cycle
Chaperones TAPBPR and tapasin associate with class-I major histocompatibility complexes (MHC-I) to promote optimization (editing) of peptide cargo. Here, we use solution NMR to investigate the mechanism of peptide exchange. We identify TAPBPR-induced conformational changes on conserved MHC-I molecul...
Tallennettuna:
| Julkaisussa: | Nat Chem Biol |
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| Päätekijät: | , , , , , , , , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
2018
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6202177/ https://ncbi.nlm.nih.gov/pubmed/29988068 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41589-018-0096-2 |
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