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• W2060324504 abstract "Understanding the specificity of protein-protein interaction mediated by domains and their ligands will have strong impact on basic and applied research. Visual inspection of WW domain sequences prompted a general classification of the domains into two large subfamilies. One subfamily contains two consecutive aromatic residues in the beta 2 strand of the domain whereas the other contains three or four consecutive aromatic residues in the same position. In the recent past, we proposed a rule of 'two vs. three aromatics' in the beta 2 strand of WW domains as a molecular discriminator between Class I and Class II WW domains, which recognize PPxY or PPLP motifs, respectively. Using phage display libraries expressing WW domains with random sequences replacing a part of the beta 2 strand, we provided additional evidence supporting our rule. We conclude that three consecutive aromatic amino acids within the beta 2 strand of WW domain are required but not always sufficient for the WW domain to belong to Class II." @default.
• W2060324504 created "2016-06-24" @default.
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• W2060324504 date "2003-11-01" @default.
• W2060324504 modified "2023-10-11" @default.
• W2060324504 title "Probing WW Domains to Uncover and Refine Determinants of Specificity in Ligand Recognition" @default.
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• W2060324504 doi "https://doi.org/10.1023/b:cyto.0000039913.56708.06" @default.
• W2060324504 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3449593" @default.
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