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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.
Plasticity of empty major histocompatibility complex class I molecules determines peptide-selector function.
Major histocompatibility complex class I (MHC I) proteins provide protection from intracellular pathogens and cancer via each of a cell's MHC I molecules binding and presenting a peptide to cytotoxic T lymphocytes. MHC I genes are highly polymorphic and can have significant diversity, with polymorphisms predominantly localised in the peptide-binding groove where they can change peptide-binding specificity. However, polymorphic residues may also determine other functional properties, such as how dependent MHC I alleles are on the peptide-loading complex for optimal acquisition of peptide cargo. We describe how differences in the peptide-binding properties of two MHC I alleles correlates with altered conformational flexibility in the peptide-empty state. We hypothesise that plasticity is an intrinsic property encoded by the protein sequence, and that co-ordinated movements of the membrane-proximal and membrane-distal domains collectively determines how dependent MHC I are on the peptide-loading complex for efficient assembly with high affinity peptides.
MHC class I, tapasin, protein plasticity, peptide selection, peptide editing
0161-5890
98-101
van Hateren, Andy
e345fa3c-d89c-4b91-947e-c1d818cc7f71
Bailey, Alistair
541e2cd9-ac72-4058-9293-def64fc2c284
Werner, Jörn M.
1b02513a-8310-4f4f-adac-dc2a466bd115
Elliott, Tim
16670fa8-c2f9-477a-91df-7c9e5b453e0e
van Hateren, Andy
e345fa3c-d89c-4b91-947e-c1d818cc7f71
Bailey, Alistair
541e2cd9-ac72-4058-9293-def64fc2c284
Werner, Jörn M.
1b02513a-8310-4f4f-adac-dc2a466bd115
Elliott, Tim
16670fa8-c2f9-477a-91df-7c9e5b453e0e

van Hateren, Andy, Bailey, Alistair, Werner, Jörn M. and Elliott, Tim (2015) Plasticity of empty major histocompatibility complex class I molecules determines peptide-selector function. Molecular Immunology, 68, (2), part A, pp. 98-101. (doi:10.1016/j.molimm.2015.03.010). (PMID:25818313).

Record type: Article

Abstract

Major histocompatibility complex class I (MHC I) proteins provide protection from intracellular pathogens and cancer via each of a cell's MHC I molecules binding and presenting a peptide to cytotoxic T lymphocytes. MHC I genes are highly polymorphic and can have significant diversity, with polymorphisms predominantly localised in the peptide-binding groove where they can change peptide-binding specificity. However, polymorphic residues may also determine other functional properties, such as how dependent MHC I alleles are on the peptide-loading complex for optimal acquisition of peptide cargo. We describe how differences in the peptide-binding properties of two MHC I alleles correlates with altered conformational flexibility in the peptide-empty state. We hypothesise that plasticity is an intrinsic property encoded by the protein sequence, and that co-ordinated movements of the membrane-proximal and membrane-distal domains collectively determines how dependent MHC I are on the peptide-loading complex for efficient assembly with high affinity peptides.

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Accepted/In Press date: 9 March 2015
e-pub ahead of print date: 26 March 2015
Published date: December 2015
Keywords: MHC class I, tapasin, protein plasticity, peptide selection, peptide editing
Organisations: Cancer Sciences

Identifiers

Local EPrints ID: 385332
URI: http://eprints.soton.ac.uk/id/eprint/385332
ISSN: 0161-5890
PURE UUID: 0695fb87-8a0b-48ca-8e8c-e219f4899eef
ORCID for Alistair Bailey: ORCID iD orcid.org/0000-0003-0023-8679
ORCID for Jörn M. Werner: ORCID iD orcid.org/0000-0002-4712-1833
ORCID for Tim Elliott: ORCID iD orcid.org/0000-0003-1097-0222

Catalogue record

Date deposited: 19 Jan 2016 10:01
Last modified: 17 Jul 2017 19:57

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Contributors

Author: Andy van Hateren
Author: Alistair Bailey ORCID iD
Author: Jörn M. Werner ORCID iD
Author: Tim Elliott ORCID iD

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