{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,30]],"date-time":"2025-10-30T22:23:11Z","timestamp":1761862991220},"reference-count":29,"publisher":"Oxford University Press (OUP)","issue":"7","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2011,4,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Motivation: The phage display peptide selection approach is widely used for defining binding specificities of globular domains. PDZ domains recognize partner proteins via C-terminal motifs and are often used as a model for interaction predictions. Here, we investigated to which extent phage display data that were recently published for 54 human PDZ domains can be applied to the prediction of human PDZ\u2013peptide interactions.<\/jats:p>\n               <jats:p>Results: Promising predictions were obtained for one-third of the 54 PDZ domains. For the other two-thirds, we detected in the phage display peptides an important bias for hydrophobic amino acids that seemed to impair correct predictions. Therefore, phage display-selected peptides may be over-hydrophobic and of high affinity, while natural interaction motifs are rather hydrophilic and mostly combine low affinity with high specificity. We suggest that potential amino acid composition bias should systematically be investigated when applying phage display data to the prediction of specific natural domain\u2013linear motif interactions.<\/jats:p>\n               <jats:p>Contact: \u00a0katja.luck@unistra.fr; gilles.trave@unistra.fr<\/jats:p>\n               <jats:p>Supplementary information: \u00a0Supplementary data are available at Bioinformatics online.<\/jats:p>","DOI":"10.1093\/bioinformatics\/btr060","type":"journal-article","created":{"date-parts":[[2011,2,8]],"date-time":"2011-02-08T05:06:38Z","timestamp":1297141598000},"page":"899-902","source":"Crossref","is-referenced-by-count":38,"title":["Phage display can select over-hydrophobic sequences that may impair prediction of natural domain\u2013peptide interactions"],"prefix":"10.1093","volume":"27","author":[{"given":"Katja","family":"Luck","sequence":"first","affiliation":[{"name":"Oncoproteins, Unit\u00e9 CNRS-UDS UMR 7242, Ecole Sup\u00e9rieure de Biotechnologie de Strasbourg, 1, Bd S\u00e9bastien Brant, BP 10413, 67412 Illkirch - Cedex, France"}]},{"given":"Gilles","family":"Trav\u00e9","sequence":"additional","affiliation":[{"name":"Oncoproteins, Unit\u00e9 CNRS-UDS UMR 7242, Ecole Sup\u00e9rieure de Biotechnologie de Strasbourg, 1, Bd S\u00e9bastien Brant, BP 10413, 67412 Illkirch - Cedex, France"}]}],"member":"286","published-online":{"date-parts":[[2011,2,7]]},"reference":[{"key":"2023012512162120900_B1","doi-asserted-by":"crossref","first-page":"12766","DOI":"10.1021\/ja060830y","article-title":"Thermodynamic basis for promiscuity and selectivity in protein-protein interactions: PDZ domains, a case study","volume":"128","author":"Basdevant","year":"2006","journal-title":"J. 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