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• W2464323932 abstract "Abstract START domain proteins are conserved α/β helix-grip fold that play a role in the non-vesicular and intracellular transport of lipids and sterols. The mechanism and conformational changes permitting the entry of the ligand into their buried binding sites is not well understood. Moreover, their functions and the identification of cognate ligands is still an active area of research. Here, we report the solution structure of STARD6 and the characterization of its backbone dynamics on multiple time-scales through 15 N spin-relaxation and amide exchange studies. We reveal for the first time the presence of concerted fluctuations in the Ω 1 loop and the C-terminal helix on the microsecond-millisecond time-scale that allows for the opening of the binding site and ligand entry. We also report that STARD6 binds specifically testosterone. Our work represents a milestone for the study of ligand binding mechanism by other START domains and the elucidation of the biological function of STARD6." @default.
• W2464323932 created "2016-07-22" @default.
• W2464323932 creator A5003947407 @default.
• W2464323932 creator A5028288558 @default.
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• W2464323932 creator A5071946741 @default.
• W2464323932 date "2016-06-24" @default.
• W2464323932 modified "2023-10-10" @default.
• W2464323932 title "STARD6 on steroids: solution structure, multiple timescale backbone dynamics and ligand binding mechanism" @default.
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• W2464323932 doi "https://doi.org/10.1038/srep28486" @default.
• W2464323932 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4919784" @default.
• W2464323932 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27340016" @default.
• W2464323932 hasPublicationYear "2016" @default.
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