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TitleAlphafold 3-guided insights into the Importinβ: Importin7 heterodimer interaction and its binding to histone H1.
Journal, issue, pagesStructure, Vol. 34, Issue 3, Page 414-425.e4, Year 2026
Publish dateMar 5, 2026
AuthorsPiotr Neumann / Olexandr Dybkov / Henning Urlaub / Ralf Ficner / Achim Dickmanns /
PubMed AbstractThe nuclear import of H1 linker histones is facilitated by a heterodimer of the transport receptors Importinβ (Impβ) and Importin7 (Imp7). The interaction between them is mediated by a stretch of C- ...The nuclear import of H1 linker histones is facilitated by a heterodimer of the transport receptors Importinβ (Impβ) and Importin7 (Imp7). The interaction between them is mediated by a stretch of C-terminal residues of Imp7 essential also for Imp7 activation by Impβ. An Impβ:Imp7:H1 complex model was predicted by Alphafold3 and validated using cross-linking data, isothermal titration calorimetry, and pull-down experiments, providing robust support for its accuracy. This model positions the H1 globular domain within the central cavity of Imp7. Refinement of this atomic model against a published cryo-electron microscopy (cryo-EM) map demonstrated significantly improved correspondence compared to the earlier interpretation, which placed the H1 globular domain within Impβ. This enhanced structural consistency further substantiates the accuracy of the AI-driven prediction. Moreover, a detailed analysis confirmed the extended C-terminal stretch of Imp7 harboring a nucleoporin-like binding (NlB) region with two FXFG-like nucleoporin motifs interacting with the outer surface of Impβ.
External linksStructure / PubMed:41529687
MethodsEM (single particle)
Resolution6.2 - 7.5 Å
Structure data

PDB-9qej:
Cryo-EM structure of the Importin beta:Importin7:Histone H1.0 complex
Method: ELECTRON MICROSCOPY / Resolution: 6.2 Å

PDB-9qf0:
Cryo-EM structure of the mportin7:Histone H1.0 complex
Method: ELECTRON MICROSCOPY / Resolution: 7.5 Å

Source
  • xenopus laevis (African clawed frog)
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Transport / Importin 7 / Importin Beta / Histone 1.0

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