ArticleThe Journal of biological chemistry2022
The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Ultratight Binding of a Capture Spiral Spider Silk Protein through Electrostatic Forces.ACS bio & med chem Au · 2026Article
- pH-triggered clustering regulates β-sheet activation in silk assembly.Communications chemistry · 2026Article
- Liquid-liquid crystalline phase separation of spider silk proteins.Communications chemistry · 2024Review
- A Minispidroin Guides the Molecular Design for Cellular Condensation Mechanisms inACS synthetic biology · 2023Article
- Factors Influencing Properties of Spider Silk Coatings and Their Interactions within a Biological Environment.Journal of functional biomaterials · 2023Review
- Recombinant protein condensation insideMaterials today. Bio · 2022Article
- 1000 spider silkomes: Linking sequences to silk physical properties.Science advances · 2022Article
- Solution Structure of Tubuliform Spidroin N-Terminal Domain and Implications for pH Dependent Dimerization.Frontiers in molecular biosciences · 2022Article
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The N-terminal (NT) domain of spider silk proteins (spidroins) is crucial for their storage at high concentrations and also regulates silk assembly. NTs from the major ampullate spidroin (MaSp) and the minor ampullate spidroin are monomeric at neutral pH and confer solubility to spidroins, whereas at lower pH, they dimerize to interconnect spidroins in a fiber. This dimerization is known to result from modulation of electrostatic interactions by protonation of well-conserved glutamates, although it is undetermined if this mechanism applies to other spidroin types as well. Here, we determine the solution and crystal structures of the flagelliform spidroin NT, which shares only 35% identity with MaSp NT, and investigate the mechanisms of its dimerization. We show that flagelliform spidroin NT is structurally similar to MaSp NT and that the electrostatic intermolecular interaction between Asp 40 and Lys 65 residues is conserved. However, the protonation events involve a different set of residues than in MaSp, indicating that an overall mechanism of pH-dependent dimerization is conserved but can be mediated by different pathways in different silk types.
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