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• W2115280552 abstract "The binding of peptide fragments of extracellular peptides to class II MHC is a crucial event in the adaptive immune response. Each MHC allotype generally binds a distinct subset of peptides and the enormous number of possible peptide epitopes prevents their complete experimental characterization. Computational methods can utilize the limited experimental data to predict the binding affinities of peptides to class II MHC.We have developed the Regularized Thermodynamic Average, or RTA, method for predicting the affinities of peptides binding to class II MHC. RTA accounts for all possible peptide binding conformations using a thermodynamic average and includes a parameter constraint for regularization to improve accuracy on novel data. RTA was shown to achieve higher accuracy, as measured by AUC, than SMM-align on the same data for all 17 MHC allotypes examined. RTA also gave the highest accuracy on all but three allotypes when compared with results from 9 different prediction methods applied to the same data. In addition, the method correctly predicted the peptide binding register of 17 out of 18 peptide-MHC complexes. Finally, we found that suboptimal peptide binding registers, which are often ignored in other prediction methods, made significant contributions of at least 50% of the total binding energy for approximately 20% of the peptides.The RTA method accurately predicts peptide binding affinities to class II MHC and accounts for multiple peptide binding registers while reducing overfitting through regularization. The method has potential applications in vaccine design and in understanding autoimmune disorders. A web server implementing the RTA prediction method is available at http://bordnerlab.org/RTA/." @default.
• W2115280552 created "2016-06-24" @default.
• W2115280552 creator A5048520206 @default.
• W2115280552 creator A5052037780 @default.
• W2115280552 date "2010-01-20" @default.
• W2115280552 modified "2023-10-07" @default.
• W2115280552 title "Prediction of the binding affinities of peptides to class II MHC using a regularized thermodynamic model" @default.
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• W2115280552 doi "https://doi.org/10.1186/1471-2105-11-41" @default.
• W2115280552 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2828437" @default.
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