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Exploring peptide/MHC detachment processes using hierarchical natural move Monte Carlo

Abstract:
Motivation: The binding between a peptide and a major histocompatibility complex (MHC) is one of the most important processes for the induction of an adaptive immune response. Many algorithms have been developed to predict peptide/MHC (pMHC) binding. However, no approach has yet been able to give structural insight into how peptides detach from the MHC. Results: In this study, we used a combination of coarse graining, hierarchical natural move Monte Carlo and stochastic conformational optimization to explore the detachment processes of 32 different peptides from HLA-A*02:01. We performed 100 independent repeats of each stochastic simulation and found that the presence of experimentally known anchor amino acids affects the detachment trajectories of our peptides. Comparison with experimental binding affinity data indicates the reliability of our approach (area under the receiver operating characteristic curve 0.85). We also compared to a 1000 ns molecular dynamics simulation of a non-binding peptide (AAAKTPVIV) and HLA-A*02:01. Even in this simulation, the longest published for pMHC, the peptide does not fully detach. Our approach is orders of magnitude faster and as such allows us to explore pMHC detachment processes in a way not possible with all-atom molecular dynamics simulations. Availability and implementation: The source code is freely available for download at http://www.cs.ox.ac.uk/mosaics/.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1093/bioinformatics/btv502

Authors


More by this author
Role:
Author
ORCID:
0000-0001-7352-3994
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Statistics
Role:
Author
ORCID:
0000-0003-1388-2252
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Computer Science
Role:
Author


Publisher:
Oxford University Press
Journal:
Bioinformatics More from this journal
Volume:
32
Issue:
2
Pages:
181-186
Place of publication:
England
Publication date:
2015-09-22
Acceptance date:
2015-08-21
DOI:
EISSN:
1367-4811
ISSN:
1367-4803
Pmid:
26395770


Language:
English
Keywords:
Pubs id:
585860
Local pid:
pubs:585860
Deposit date:
2021-03-16

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