Plasticity of empty major histocompatibility complex class I molecules determines peptide-selector function

Plasticity of empty major histocompatibility complex class I molecules determines peptide-selector function

•MHC class I alleles vary in their intrinsic ability to select optimal peptides.•Ability of MHC to self-assemble is inversely correlated with dependence on tapasin.•Variation in peptide selector function correlates with the plasticity of empty MHC.•Increased plasticity of empty MHC I allows more eff...

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Main Authors: van Hateren, Andy, Bailey, Alistair, Werner, Jörn M., Elliott, Tim
Format: Online
Language:English
Published: Pergamon Press 2015
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4726658/
id pubmed-4726658
recordtype oai_dc
spelling pubmed-47266582016-02-22 Plasticity of empty major histocompatibility complex class I molecules determines peptide-selector function van Hateren, Andy Bailey, Alistair Werner, Jörn M. Elliott, Tim Review •MHC class I alleles vary in their intrinsic ability to select optimal peptides.•Ability of MHC to self-assemble is inversely correlated with dependence on tapasin.•Variation in peptide selector function correlates with the plasticity of empty MHC.•Increased plasticity of empty MHC I allows more efficient peptide selector function.•Co-ordinated domain–domain movements contribute to determine plasticity. Pergamon Press 2015-12 /pmc/articles/PMC4726658/ /pubmed/25818313 http://dx.doi.org/10.1016/j.molimm.2015.03.010 Text en © 2015 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author van Hateren, Andy
Bailey, Alistair
Werner, Jörn M.
Elliott, Tim
spellingShingle van Hateren, Andy
Bailey, Alistair
Werner, Jörn M.
Elliott, Tim
Plasticity of empty major histocompatibility complex class I molecules determines peptide-selector function
author_facet van Hateren, Andy
Bailey, Alistair
Werner, Jörn M.
Elliott, Tim
author_sort van Hateren, Andy
title Plasticity of empty major histocompatibility complex class I molecules determines peptide-selector function
title_short Plasticity of empty major histocompatibility complex class I molecules determines peptide-selector function
title_full Plasticity of empty major histocompatibility complex class I molecules determines peptide-selector function
title_fullStr Plasticity of empty major histocompatibility complex class I molecules determines peptide-selector function
title_full_unstemmed Plasticity of empty major histocompatibility complex class I molecules determines peptide-selector function
title_sort plasticity of empty major histocompatibility complex class i molecules determines peptide-selector function
description •MHC class I alleles vary in their intrinsic ability to select optimal peptides.•Ability of MHC to self-assemble is inversely correlated with dependence on tapasin.•Variation in peptide selector function correlates with the plasticity of empty MHC.•Increased plasticity of empty MHC I allows more efficient peptide selector function.•Co-ordinated domain–domain movements contribute to determine plasticity.
publisher Pergamon Press
publishDate 2015
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4726658/
_version_ 1613528384352026624

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