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


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).

Download

[img] PDF 2015 Plasticity of empty major histocompatibility complex class I molecules determines peptide selector function.pdf - Version of Record
Available under License Creative Commons Attribution.

Download (605kB)

Description/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.

Item Type: Article
Digital Object Identifier (DOI): doi:10.1016/j.molimm.2015.03.010
ISSNs: 0161-5890 (print)
Keywords: MHC class I, tapasin, protein plasticity, peptide selection, peptide editing
Organisations: Cancer Sciences
ePrint ID: 385332
Date :
Date Event
9 March 2015Accepted/In Press
26 March 2015e-pub ahead of print
December 2015Published
Date Deposited: 19 Jan 2016 10:01
Last Modified: 22 Feb 2017 07:05
Further Information:Google Scholar
URI: http://eprints.soton.ac.uk/id/eprint/385332

Actions (login required)

View Item View Item