Cargando…
A loop structure allows TAPBPR to exert its dual function as MHC I chaperone and peptide editor
Adaptive immunity vitally depends on major histocompatibility complex class I (MHC I) molecules loaded with peptides. Selective loading of peptides onto MHC I, referred to as peptide editing, is catalyzed by tapasin and the tapasin-related TAPBPR. An important catalytic role has been ascribed to a s...
Autores principales: | Sagert, Lina, Hennig, Felix, Thomas, Christoph, Tampé, Robert |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7117912/ https://www.ncbi.nlm.nih.gov/pubmed/32167472 http://dx.doi.org/10.7554/eLife.55326 |
Ejemplares similares
-
The ER folding sensor UGGT1 acts on TAPBPR-chaperoned peptide-free MHC I
por: Sagert, Lina, et al.
Publicado: (2023) -
Chaperone function in antigen presentation by MHC class I molecules—tapasin in the PLC and TAPBPR beyond
por: Margulies, David H., et al.
Publicado: (2023) -
TAPBPR alters MHC class I peptide presentation by functioning as a peptide exchange catalyst
por: Hermann, Clemens, et al.
Publicado: (2015) -
Peptide exchange on MHC-I by TAPBPR is driven by a negative allostery release cycle
por: McShan, Andrew C., et al.
Publicado: (2018) -
TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap
por: McShan, Andrew C., et al.
Publicado: (2021)