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• W2086177790 abstract "We present herein a review of our recent results on the characterization of the binding sites of STARD1, STARD5 and STARD6 using NMR and other biophysical techniques. Whereas STARD1 and STARD6 bind cholesterol, no cholesterol binding could be detected for STARD5. However, titration of STARD5 with cholic acid and chenodeoxycholic acid led to specific binding. Using perturbation of the (1)H-(15)N-HSQC spectra and the sequence specific NMR assignments, we identified the amino acids in contact with those ligands. The most perturbed residues in presence of ligands are lining the internal cavity of the protein. Interestingly, these residues are not conserved in STARD1 and STARD6 and could therefore be key structural determinants of the specificity of START domains toward their ligands. We highlight three tissues expressing STARD5 that are affected by bile acids." @default.
• W2086177790 created "2016-06-24" @default.
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• W2086177790 date "2013-05-01" @default.
• W2086177790 modified "2023-10-16" @default.
• W2086177790 title "STARD5 specific ligand binding: Comparison with STARD1 and STARD4 subfamilies" @default.
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• W2086177790 doi "https://doi.org/10.1016/j.mce.2013.01.004" @default.
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