ArticleScientific reports2016
STARD6 on steroids: solution structure, multiple timescale backbone dynamics and ligand binding mechanism.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 31 citations in OpenAlex.
- Getting a grip on StAR-related lipid-transfer (START) domain proteins in bacteria.FEMS microbiology reviews · 2026Review
- Differential regulation of STARD1, STARD4 and STARD6 in the human ovary.The Journal of endocrinology · 2024Article
- Allosterically coupled conformational dynamics in solution prepare the sterol transfer protein StarD4 to release its cargo upon interaction with target membranes.Frontiers in molecular biosciences · 2023Article
- Retrospective study for the universal applicability of the residue-based linear free energy relationship in the two-state exchange of protein molecules.Scientific reports · 2022Article
- Allosteric regulation of thioesterase superfamily member 1 by lipid sensor domain binding fatty acids and lysophosphatidylcholine.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Association analysis of polymorphisms inNeuropsychiatric disease and treatment · 2019Article
- Structural basis of sterol binding and transport by a yeast StARkin domain.The Journal of biological chemistry · 2018Article
- Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Thirty-Eight-Year Follow-Up of Two Sibling Lipoid Congenital Adrenal Hyperplasia Patients Due to Homozygous Steroidogenic Acute Regulatory (STARD1) Protein Mutation. Molecular Structure and Modeling of the STARD1 L275P Mutation.Frontiers in neuroscience · 2016Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
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 Ω1 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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.