ArticleProtein science : a publication of the Protein Society2011
Propensity for C-terminal domain swapping correlates with increased regional flexibility in the C-terminus of RNase A.
Article in Protein science : a publication of the Protein Society, 2011. 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.
- Characterization of protein unfolding by fast cross-linking mass spectrometry using di-ortho-phthalaldehyde cross-linkers.Nature communications · 2022Article
- A Simple Model of Protein Domain Swapping in Crowded Cellular Environments.Biophysical journal · 2016Article
- Evidences for the unfolding mechanism of three-dimensional domain swapping.Protein science : a publication of the Protein Society · 2013Article
- Foldon unfolding mediates the interconversion between M(pro)-C monomer and 3D domain-swapped dimer.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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2 authors.
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Abstract
Domain swapping is a type of oligomerization in which monomeric proteins exchange a structural element, resulting in oligomers whose subunits recapitulate the native, monomeric fold. It has been implicated as a potential mechanism for protein aggregation, which provides a strong impetus to understand the structural determinants and folding mechanisms that trigger domain swapping. Bovine pancreatic ribonuclease A (RNase A) is a well-studied protein known to domain swap under extreme conditions, such as lyophilization from acetic acid. The major domain-swapped dimer form of RNase A exchanges a β-strand at its C-terminus to form a C-terminal domain-swapped dimer. To study the mechanism by which C-terminal swapping occurs, we used a variant of RNase A containing a P114G mutation that readily domain swaps under physiological conditions. Using NMR and hydrogen-deuterium exchange, we find that the P114G variant has decreased protection from hydrogen exchange compared to the wild-type protein near the C-terminal hinge region. Our results suggest that domain swapping occurs via a local high-energy fluctuation at the C-terminus.
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Registered trials
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