Fig. 3: Binding details of Spindlin1-HBx2-21 complex and mutagenesis studies. | Nature Communications

Fig. 3: Binding details of Spindlin1-HBx2-21 complex and mutagenesis studies.

From: Molecular insights into Spindlin1-HBx interplay and its impact on HBV transcription from cccDNA minichromosome

Fig. 3

a Hydrophobic interface between Spindlin1 (surface view in light gray) and HBx2-21 (ribbon view in yellow) with hydrophobic residues showing dots. b Parallel β-sheet formed by β1 strand (yellow) of HBx2–21 and β4 strand (pink) of Spindlin1 Tudor 3. c Parallel β-sheet formed between β1 of Spindlin1 Tudor 3 and β2 of HBx2–21. (b-c) Blue dashes: direct hydrogen bonds or salt bridges. d Hydrophobic core formed by Spindlin1 K216, V218, V232, I245, L258 (shown as stick in pink) and HBx M5, L16, L18 (shown as stick in yellow). e ITC fitting curves of HBx2–21 peptide titrated to Spindlin150–262 Tudor 3 mutants. f ITC fitting curves of mutant HBx2–21 peptides titrated to Spindlin150–262. N.D., not detectable.

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