ArticleProceedings of the National Academy of Sciences of the United States of America2001
Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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72 citing papers in PubMed, 205 citations in OpenAlex.
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- Dimerization of natively folded molecules drives misfolding and aggregation in Cys-depleted variants of cataract-associated human lens γD-crystallin.bioRxiv : the preprint server for biology · 2026Article
- Insights into mechanisms and significance of domain swapping from emerging examples in the Mog1p/PsbP-like fold.Biochemical and biophysical research communications · 2025Review
- Phase separation-based visualization of protein-protein interactions and kinase activities in plants.The Plant cell · 2023Article
- GRB2 dimerization mediated by SH2 domain-swapping is critical for T cell signaling and cytokine production.Scientific reports · 2023Article
- Heterotypic Amyloid β interactions facilitate amyloid assembly and modify amyloid structure.The EMBO journal · 2022Article
- Single-molecule optical tweezers reveals folding steps of the domain swapping mechanism of a protein.Biophysical journal · 2021Article
- Human FoxP Transcription Factors as Tractable Models of the Evolution and Functional Outcomes of Three-Dimensional Domain Swapping.International journal of molecular sciences · 2021Review
- Protein yoga: Conformational versatility of the Hemolysin II C-terminal domain detailed by NMR structures for multiple states.Protein science : a publication of the Protein Society · 2021Article
- Exposing the distinctive modular behavior of β-strands and α-helices in folded proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Monothiol and dithiol glutaredoxin-1 fromIUCrJ · 2020Article
- Ameliorating amyloid aggregation through osmolytes as a probable therapeutic molecule against Alzheimer's disease and type 2 diabetes.RSC advances · 2020Article
- 3D domain swapping in the TIM barrel of the α subunit of Streptococcus pneumoniae tryptophan synthase.Acta crystallographica. Section D, Structural biology · 2020Article
- Acquired rare recurrentAmerican journal of cancer research · 2020Article
- Adaption of human antibody λ and κ light chain architectures to CDR repertoires.Protein engineering, design & selection : PEDS · 2019Article
- The non-swapped monomeric structure of the arginine-binding protein from Thermotoga maritima.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Tandem domain swapping: determinants of multidomain protein misfolding.Current opinion in structural biology · 2019Review
- Studies of the oligomerisation mechanism of a cystatin-based engineered protein scaffold.Scientific reports · 2019Article
- Prolines Affect the Nucleation Phase of Amyloid Fibrillation Reaction; Mutational Analysis of Human Stefin B.ACS chemical neuroscience · 2019Article
- A five-residue motif for the design of domain swapping in proteins.Nature communications · 2019Article
12 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
p13suc1 has two native states, a monomer and a domain-swapped dimer. We show that their folding pathways are connected by the denatured state, which introduces a kinetic barrier between monomer and dimer under native conditions. The barrier is lowered under conditions that speed up unfolding, thereby allowing, to our knowledge for the first time, a quantitative dissection of the energetics of domain swapping. The monomer-dimer equilibrium is controlled by two conserved prolines in the hinge loop that connects the exchanging domains. These two residues exploit backbone strain to specifically direct dimer formation while preventing higher-order oligomerization. Thus, the loop acts as a loaded molecular spring that releases tension in the monomer by adopting its alternative conformation in the dimer. There is an excellent correlation between domain swapping and aggregation, suggesting they share a common mechanism. These insights have allowed us to redesign the domain-swapping propensity of suc1 from a fully monomeric to a fully dimeric protein.
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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.