ArticleBioscience reports2018
Combinatorial use of disulfide bridges and native sulfur-SAD phasing for rapid structure determination of coiled-coils.
Article in Bioscience reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- A coiled-coil-based design strategy for the thermostabilization of G-protein-coupled receptors.Scientific reports · 2023Article
- Structural insights into plasmalemma vesicle-associated protein (PLVAP): Implications for vascular endothelial diaphragms and fenestrae.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Addressing the Molecular Mechanism of Longitudinal Lamin Assembly Using Chimeric Fusions.Cells · 2020Article
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3 authors.
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Abstract
Coiled-coils are ubiquitous protein-protein interaction motifs found in many eukaryotic proteins. The elongated, flexible and often irregular nature of coiled-coils together with their tendency to form fibrous arrangements in crystals imposes challenges on solving the phase problem by molecular replacement. Here, we report the successful combinatorial use of native and rational engineered disulfide bridges together with sulfur-SAD phasing as a powerful tool to stabilize and solve the structure of coiled-coil domains in a straightforward manner. Our study is a key example of how modern sulfur SAD combined with mutagenesis can help to advance and simplify the structural study of challenging coiled-coil domains by X-ray crystallography.
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