Abstract:
:Large-scale interaction studies contribute the largest fraction of protein interactions information in databases. However, co-purification of non-specific or indirect ligands, often results in data sets that are affected by a considerable number of false positives. For the fraction of interactions mediated by short linear peptides, we present here a combined experimental and computational strategy for ranking the reliability of the inferred partners. We apply this strategy to the family of 14-3-3 domains. We have first characterized the recognition specificity of this domain family, largely confirming the results of previous analyses, while revealing new features of the preferred sequence context of 14-3-3 phospho-peptide partners. Notably, a proline next to the carboxy side of the phospho-amino acid functions as a potent inhibitor of 14-3-3 binding. The position-specific information about residue preference was encoded in a scoring matrix and two regular expressions. The integration of these three features in a single predictive model outperforms publicly available prediction tools. Next we have combined, by a naïve Bayesian approach, these "peptide features" with "protein features", such as protein co-expression and co-localization. Our approach provides an orthogonal reliability assessment and maps with high confidence the 14-3-3 peptide target on the partner proteins.
journal_name
Proteomicsjournal_title
Proteomicsauthors
Panni S,Montecchi-Palazzi L,Kiemer L,Cabibbo A,Paoluzi S,Santonico E,Landgraf C,Volkmer-Engert R,Bachi A,Castagnoli L,Cesareni Gdoi
10.1002/pmic.201000030subject
Has Abstractpub_date
2011-01-01 00:00:00pages
128-43issue
1eissn
1615-9853issn
1615-9861journal_volume
11pub_type
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