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These domains are classified into classes I, II and III, depending on their binding partners and the nature of bonds formed. Binding specificities of PDZ domains are very crucial in order to understand the complexity of signaling pathways. It is still an open question how these domains recognize and bind their partners.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Results<\/jats:title>\n            <jats:p>The focus of the current study is two folds: 1) predicting to which peptides a PDZ domain will bind and 2) classification of PDZ domains, as Class I, II or I-II, given the primary sequences of the PDZ domains. Trigram and bigram amino acid frequencies are used as features in machine learning methods. Using 85 PDZ domains and 181 peptides, our model reaches high prediction accuracy (91.4%) for binary interaction prediction which outperforms previously investigated similar methods. Also, we can predict classes of PDZ domains with an accuracy of 90.7%. We propose three critical amino acid sequence motifs that could have important roles on specificity pattern of PDZ domains.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Conclusions<\/jats:title>\n            <jats:p>Our model on PDZ interaction dataset shows that our approach produces encouraging results. The method can be further used as a virtual screening technique to reduce the search space for putative candidate target proteins and drug-like molecules of PDZ domains.<\/jats:p>\n          <\/jats:sec>","DOI":"10.1186\/1471-2105-11-357","type":"journal-article","created":{"date-parts":[[2010,6,30]],"date-time":"2010-06-30T18:14:47Z","timestamp":1277921687000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":42,"title":["Interaction prediction and classification of PDZ domains"],"prefix":"10.1186","volume":"11","author":[{"given":"Sibel","family":"Kalyoncu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ozlem","family":"Keskin","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Attila","family":"Gursoy","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2010,6,30]]},"reference":[{"issue":"4","key":"3814_CR1","doi-asserted-by":"publisher","first-page":"1225","DOI":"10.1021\/cr040409x","volume":"108","author":"Z Keskin","year":"2008","unstructured":"Keskin Z, Gursoy A, Ma B, Nussinov R: Principles of protein-protein interactions: What are the preferred ways for proteins to interact? 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