ArticleBiophysical chemistry
Structural landscape of the proline-rich domain of Sos1 nucleotide exchange factor.
Article in Biophysical chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed.
- Positive feedback in Ras activation by full-length SOS arises from autoinhibition release mechanism.Biophysical journal · 2024Article
- Kinetic frustration by limited bond availability controls the LAT protein condensation phase transition on membranes.Science advances · 2022Article
- Allosteric regulation of GRB2 modulates RAS activation.Small GTPases · 2022Article
- Article
- Mechanism of SOS PR-domain autoinhibition revealed by single-molecule assays on native protein from lysate.Nature communications · 2017Article
- Digested disorder: Quarterly intrinsic disorder digest (April-May-June, 2013).Intrinsically disordered proteinsReview
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Despite its key role in mediating a plethora of cellular signaling cascades pertinent to health and disease, little is known about the structural landscape of the proline-rich (PR) domain of Sos1 guanine nucleotide exchange factor. Herein, using a battery of biophysical tools, we provide evidence that the PR domain of Sos1 is structurally disordered and adopts an extended random coil-like conformation in solution. Of particular interest is the observation that while chemical denaturation of PR domain results in the formation of a significant amount of polyproline II (PPII) helices, it has little or negligible effect on its overall size as measured by its hydrodynamic radius. Our data also show that the PR domain displays a highly dynamic conformational basin in agreement with the knowledge that the intrinsically unstructured proteins rapidly interconvert between an ensemble of conformations. Collectively, our study provides new insights into the conformational equilibrium of a key signaling molecule with important consequences on its physiological function.
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