ArticleScientific reports2016
Acidic Residues Control the Dimerization of the N-terminal Domain of Black Widow Spiders' Major Ampullate Spidroin 1.
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 14 papers.
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Who cites it
14 citing papers in PubMed, 36 citations in OpenAlex.
- Sequence-encoded tubular architectures in disordered spider silk proteins revealed by multiscale simulations and NMR.PNAS nexus · 2025Article
- Nanostructured Protein Surfaces Inspired by Spider Silk.Advanced materials (Deerfield Beach, Fla.) · 2025Review
- Influence of Spider Silk Protein Structure on Mechanical and Biological Properties for Energetic Material Detection.Molecules (Basel, Switzerland) · 2024Review
- Unusual pBiomacromolecules · 2023Article
- Molecular mechanisms of the high performance of spider silks revealed through multi-omics analysis.Biophysics and physicobiology · 2023Article
- Complexity of Spider Dragline Silk.Biomacromolecules · 2022Review
- The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence.The Journal of biological chemistry · 2022Article
- Solution Structure of Tubuliform Spidroin N-Terminal Domain and Implications for pH Dependent Dimerization.Frontiers in molecular biosciences · 2022Article
- Interplay of Different Major Ampullate Spidroins during Assembly and Implications for Fiber Mechanics.Advanced materials (Deerfield Beach, Fla.) · 2021Article
- Clinical characteristics of patients with black widow spider bites: A report of 59 patients and single-center experience.World journal of emergency medicine · 2021Article
- Structural Characterization of Black Widow Spider Dragline Silk Proteins CRP1 and CRP4.Molecules (Basel, Switzerland) · 2020Article
- The effect of terminal globular domains on the response of recombinant mini-spidroins to fiber spinning triggers.Scientific reports · 2020Article
- Structural Basis of Oligomerization of N-Terminal Domain of Spider Aciniform Silk Protein.International journal of molecular sciences · 2020Article
- Chemical Synthesis of Silk-Mimetic Polymers.Materials (Basel, Switzerland) · 2019Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dragline silk is the most prominent amongst spider silks and comprises two types of major ampullate spidroins (MaSp) differing in their proline content. In the natural spinning process, the conversion of soluble MaSp into a tough fiber is, amongst other factors, triggered by dimerization and conformational switching of their helical amino-terminal domains (NRN). Both processes are induced by protonation of acidic residues upon acidification along the spinning duct. Here, the structure and monomer-dimer-equilibrium of the domain NRN1 of Latrodectus hesperus MaSp1 and variants thereof have been investigated, and the key residues for both could be identified. Changes in ionic composition and strength within the spinning duct enable electrostatic interactions between the acidic and basic pole of two monomers which prearrange into an antiparallel dimer. Upon naturally occurring acidification this dimer is stabilized by protonation of residue E114. A conformational change is independently triggered by protonation of clustered acidic residues (D39, E76, E81). Such step-by-step mechanism allows a controlled spidroin assembly in a pH- and salt sensitive manner, preventing premature aggregation of spider silk proteins in the gland and at the same time ensuring fast and efficient dimer formation and stabilization on demand in the spinning duct.
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