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• W2010167497 abstract "Tandem PDZ domains have been suggested to form structurally independent supramodules. However, dissimilarity between crystallography and NMR models emphasize their malleable conformation. Studies in full-length scaffold proteins are needed to examine the effect of tertiary interactions within their native context. Using single-molecule fluorescence to characterize the N-terminal PDZ tandem in PSD-95, we provide the first direct evidence that PDZ tandems can be structurally independent within a full-length scaffold protein. Molecular refinement using our data converged on a single structure with an antiparallel alignment of the ligand-binding sites. Devoid of interaction partners, single-molecule conditions captured PSD-95 in its unbound, ground state. Interactions between PDZ domains could not be detected while fluctuation correlation spectroscopy showed that other conformations are dynamically sampled. We conclude that ultra-weak interactions stabilize the conformation providing a low-relief energy landscape that allows the domain orientation to be flipped by environmental interactions." @default.
• W2010167497 created "2016-06-24" @default.
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• W2010167497 date "2011-06-01" @default.
• W2010167497 modified "2023-10-17" @default.
• W2010167497 title "Domain Orientation in the N-Terminal PDZ Tandem from PSD-95 Is Maintained in the Full-Length Protein" @default.
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• W2010167497 doi "https://doi.org/10.1016/j.str.2011.02.017" @default.
• W2010167497 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3116789" @default.
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