The role of MHC I protein dynamics in tapasin and TAPBPR-assisted immunopeptidome editing
The role of MHC I protein dynamics in tapasin and TAPBPR-assisted immunopeptidome editing
Major Histocompatibility Complex class I (MHC I) molecules are highly polymorphic, with allotypes differing in peptide binding preferences, and in their dependence upon tapasin for optimal peptide selection. The tapasin dependence of MHC allotypes is inversely correlated with their self-editing ability, and underpinned by conformational plasticity. Recently, TAPBPR has been shown to enhance MHC I assembly via a chaperone-like function, and by editing the peptide repertoire of some MHC I allotypes. Structural analysis has shown TAPBPR binding changes the conformation and dynamics of MHC I, with MHC protein dynamics likely to determine the prevailing TAPBPR function: generically enhancing MHC I assembly by stabilising highly dynamic peptide-empty MHC I; and by editing the peptide repertoire of highly dynamic MHC I allotypes.
138-143
van Hateren, Andy
e345fa3c-d89c-4b91-947e-c1d818cc7f71
Elliott, Timothy
16670fa8-c2f9-477a-91df-7c9e5b453e0e
12 July 2021
van Hateren, Andy
e345fa3c-d89c-4b91-947e-c1d818cc7f71
Elliott, Timothy
16670fa8-c2f9-477a-91df-7c9e5b453e0e
van Hateren, Andy and Elliott, Timothy
(2021)
The role of MHC I protein dynamics in tapasin and TAPBPR-assisted immunopeptidome editing.
Current Opinion in Immunology, 70, .
(doi:10.1016/j.coi.2021.06.016).
Abstract
Major Histocompatibility Complex class I (MHC I) molecules are highly polymorphic, with allotypes differing in peptide binding preferences, and in their dependence upon tapasin for optimal peptide selection. The tapasin dependence of MHC allotypes is inversely correlated with their self-editing ability, and underpinned by conformational plasticity. Recently, TAPBPR has been shown to enhance MHC I assembly via a chaperone-like function, and by editing the peptide repertoire of some MHC I allotypes. Structural analysis has shown TAPBPR binding changes the conformation and dynamics of MHC I, with MHC protein dynamics likely to determine the prevailing TAPBPR function: generically enhancing MHC I assembly by stabilising highly dynamic peptide-empty MHC I; and by editing the peptide repertoire of highly dynamic MHC I allotypes.
Text
20210616 Current Opinions resubmission COIMMU-D-20-00084_R1
- Accepted Manuscript
More information
Accepted/In Press date: 24 June 2021
e-pub ahead of print date: 12 July 2021
Published date: 12 July 2021
Additional Information:
Funding Information:
This work was supported by Cancer Research UK Program award A28279. The authors declare that they have no conflicts of interest. This review is dedicated to the memories of Vincenzo Cerundolo and Nilabh Shastri.
Publisher Copyright:
© 2021
Identifiers
Local EPrints ID: 450785
URI: http://eprints.soton.ac.uk/id/eprint/450785
ISSN: 0952-7915
PURE UUID: 05934957-fe4e-4845-b71d-ed74af7249cf
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Date deposited: 11 Aug 2021 16:31
Last modified: 17 Mar 2024 06:46
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