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...

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Detalles Bibliográficos
Autores principales: McShan, Andrew C., Natarajan, Kannan, Kumirov, Vlad K., Flores-Solis, David, Jiang, Jiansheng, Badstübner, Mareike, Toor, Jugmohit S., Bagshaw, Clive R., Kovrigin, Evgenii L., Margulies, David H., Sgourakis, Nikolaos G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2018
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6202177/
https://www.ncbi.nlm.nih.gov/pubmed/29988068
http://dx.doi.org/10.1038/s41589-018-0096-2

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6202177/
https://www.ncbi.nlm.nih.gov/pubmed/29988068
http://dx.doi.org/10.1038/s41589-018-0096-2

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