TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap

The molecular chaperones tapasin and TAPBPR play important roles in defining the repertoire of peptides displayed by MHC class I. Here, the authors combine NMR, ITC, fluorescence polarization measurements and deep mutational scanning analyses to reveal a peptide editing mechanism, where the G24-R36...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Andrew C. McShan, Christine A. Devlin, Giora I. Morozov, Sarah A. Overall, Danai Moschidi, Neha Akella, Erik Procko, Nikolaos G. Sgourakis
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/307b0a46ed7d4915b4300973f40e73c1
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:307b0a46ed7d4915b4300973f40e73c1
record_format	dspace
spelling	oai:doaj.org-article:307b0a46ed7d4915b4300973f40e73c12021-12-02T14:47:28ZTAPBPR promotes antigen loading on MHC-I molecules using a peptide trap10.1038/s41467-021-23225-62041-1723https://doaj.org/article/307b0a46ed7d4915b4300973f40e73c12021-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-23225-6https://doaj.org/toc/2041-1723The molecular chaperones tapasin and TAPBPR play important roles in defining the repertoire of peptides displayed by MHC class I. Here, the authors combine NMR, ITC, fluorescence polarization measurements and deep mutational scanning analyses to reveal a peptide editing mechanism, where the G24-R36 loop in TAPBPR acts as a molecular trap to promote the selection of high-affinity peptide cargo.Andrew C. McShanChristine A. DevlinGiora I. MorozovSarah A. OverallDanai MoschidiNeha AkellaErik ProckoNikolaos G. SgourakisNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Andrew C. McShan Christine A. Devlin Giora I. Morozov Sarah A. Overall Danai Moschidi Neha Akella Erik Procko Nikolaos G. Sgourakis TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap
description	The molecular chaperones tapasin and TAPBPR play important roles in defining the repertoire of peptides displayed by MHC class I. Here, the authors combine NMR, ITC, fluorescence polarization measurements and deep mutational scanning analyses to reveal a peptide editing mechanism, where the G24-R36 loop in TAPBPR acts as a molecular trap to promote the selection of high-affinity peptide cargo.
format	article
author	Andrew C. McShan Christine A. Devlin Giora I. Morozov Sarah A. Overall Danai Moschidi Neha Akella Erik Procko Nikolaos G. Sgourakis
author_facet	Andrew C. McShan Christine A. Devlin Giora I. Morozov Sarah A. Overall Danai Moschidi Neha Akella Erik Procko Nikolaos G. Sgourakis
author_sort	Andrew C. McShan
title	TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap
title_short	TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap
title_full	TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap
title_fullStr	TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap
title_full_unstemmed	TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap
title_sort	tapbpr promotes antigen loading on mhc-i molecules using a peptide trap
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/307b0a46ed7d4915b4300973f40e73c1
work_keys_str_mv	AT andrewcmcshan tapbprpromotesantigenloadingonmhcimoleculesusingapeptidetrap AT christineadevlin tapbprpromotesantigenloadingonmhcimoleculesusingapeptidetrap AT gioraimorozov tapbprpromotesantigenloadingonmhcimoleculesusingapeptidetrap AT sarahaoverall tapbprpromotesantigenloadingonmhcimoleculesusingapeptidetrap AT danaimoschidi tapbprpromotesantigenloadingonmhcimoleculesusingapeptidetrap AT nehaakella tapbprpromotesantigenloadingonmhcimoleculesusingapeptidetrap AT erikprocko tapbprpromotesantigenloadingonmhcimoleculesusingapeptidetrap AT nikolaosgsgourakis tapbprpromotesantigenloadingonmhcimoleculesusingapeptidetrap
_version_	1718389501258104832

TAPBPR promotes antigen loading on MHC-I molecules using a peptide trap

Ejemplares similares