TY - JOUR
T1 - Predicting proteasomal cleavage sites: a comparison of available methods
AU - Saxová, Patricia
AU - Buus, Søren
AU - Brunak, Søren
AU - Kesmir, Can
N1 - Keywords: Algorithms; Amino Acid Sequence; Computational Biology; Computer Simulation; Cysteine Endopeptidases; Databases, Protein; Epitopes; HLA-A Antigens; HLA-B Antigens; Humans; Molecular Sequence Data; Multienzyme Complexes; Peptides; Proteasome Endopeptidase Complex; Proteins; Sequence Analysis, Protein
PY - 2003
Y1 - 2003
N2 - The proteasome plays an essential role in the immune responses of vertebrates. By degrading intercellular proteins from self and non-self, the proteasome produces the majority of the peptides that are presented to cytotoxic T cells (CTL). There is accumulating evidence that the C-terminal, in particular, of CTL epitopes is cleaved precisely by the proteasome, whereas the N-terminal is produced with an extension, and later trimmed by peptidases in the cytoplasm and in the endoplasmic reticulum. Recently, three publicly available methods have been developed for prediction of the specificity of the proteasome. Here, we compare the performance of these methods on a large set of CTL epitopes. The best method, NetChop at www.cbs.dtu.dk/Services/NetChop, can capture approximately 70% of the C-termini correctly. This result suggests that the predictions can still be improved, particularly if more quantitative degradation data become available.
AB - The proteasome plays an essential role in the immune responses of vertebrates. By degrading intercellular proteins from self and non-self, the proteasome produces the majority of the peptides that are presented to cytotoxic T cells (CTL). There is accumulating evidence that the C-terminal, in particular, of CTL epitopes is cleaved precisely by the proteasome, whereas the N-terminal is produced with an extension, and later trimmed by peptidases in the cytoplasm and in the endoplasmic reticulum. Recently, three publicly available methods have been developed for prediction of the specificity of the proteasome. Here, we compare the performance of these methods on a large set of CTL epitopes. The best method, NetChop at www.cbs.dtu.dk/Services/NetChop, can capture approximately 70% of the C-termini correctly. This result suggests that the predictions can still be improved, particularly if more quantitative degradation data become available.
M3 - Journal article
C2 - 12807816
SN - 0953-8178
VL - 15
SP - 781
EP - 787
JO - International Immunology
JF - International Immunology
IS - 7
ER -