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• W3033408046 abstract "Abstract Conformationally flexible protein complexes represent a major challenge for structural and dynamical studies. We present herein a method based on a hybrid NMR/MD approach to characterize the complex formed between the disordered p53TAD 1–60 and the metastasis‐associated S100A4. Disorder‐to‐order transitions of both TAD1 and TAD2 subdomains upon interaction is detected. Still, p53TAD 1–60 remains highly flexible in the bound form, with residues L26, M40, and W53 being anchored to identical hydrophobic pockets of the S100A4 monomer chains. In the resulting “fuzzy” complex, the clamp‐like binding of p53TAD 1–60 relies on specific hydrophobic anchors and on the existence of extended flexible segments. Our results demonstrate that structural and dynamical NMR parameters (cumulative Δ δ , SSP, temperature coefficients, relaxation time, hetNOE) combined with MD simulations can be used to build a structural model even if, due to high flexibility, the classical solution structure calculation is not possible." @default.
• W3033408046 created "2020-06-12" @default.
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• W3033408046 date "2020-07-22" @default.
• W3033408046 modified "2023-09-26" @default.
• W3033408046 title "Tumor‐Suppressor p53TAD^1–60 Forms a Fuzzy Complex with Metastasis‐Associated S100A4: Structural Insights and Dynamics by an NMR/MD Approach" @default.
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• W3033408046 doi "https://doi.org/10.1002/cbic.202000348" @default.
• W3033408046 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7689910" @default.
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