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• W2000251153 endingPage "93" @default.
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• W2000251153 abstract "PDZ domain interactions are involved in signaling and trafficking pathways that coordinate crucial cellular processes. Alignment-based PDZ binding motifs identify the few most favorable residues at certain positions along the peptide backbone. However, sequences that bind the CAL (CFTR-associated ligand) PDZ domain reveal only a degenerate motif that overpredicts the true number of high-affinity interactors. Here, we combine extended peptide-array motif analysis with biochemical techniques to show that non-motif “modulator” residues influence CAL binding. The crystallographic structures of 13 CAL:peptide complexes reveal defined, but accommodating stereochemical environments at non-motif positions, which are reflected in modulator preferences uncovered by multisequence substitutional arrays. These preferences facilitate the identification of high-affinity CAL binding sequences and differentially affect CAL and NHERF PDZ binding. As a result, they also help determine the specificity of a PDZ domain network that regulates the trafficking of CFTR at the apical membrane." @default.
• W2000251153 created "2016-06-24" @default.
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• W2000251153 date "2014-01-01" @default.
• W2000251153 modified "2023-10-14" @default.
• W2000251153 title "Stereochemical Preferences Modulate Affinity and Selectivity among Five PDZ Domains that Bind CFTR: Comparative Structural and Sequence Analyses" @default.
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• W2000251153 doi "https://doi.org/10.1016/j.str.2013.09.019" @default.
• W2000251153 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3947174" @default.
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