Fig. 4 | Nature Communications

Fig. 4

From: Functional activity of the H3.3 histone chaperone complex HIRA requires trimerization of the HIRA subunit

Fig. 4The alternative text for this image may have been generated using AI.

Crystal structure of HIRA(644–1017) reveals a homotrimer. a Overall structure of homotrimeric HIRA(644–1017). Subunits A, B and C are shown in light green, emerald green, and blue, respectively. The loop regions (860–907) are shown in red. b Structure of the HIRA monomer. The β1 and β2 motifs are shown in pink and yellow, respectively. The α-helical domain and the loop region are shown in white and red, respectively. Black triangles indicate residue numbers of HIRA(644–1017). c Trp799 located at the interface between subunits A and B (emerald green). d The CABIN1-binding loop shown in red and highlighting Phe870 and Arg871. The side chain of Arg871 was not visible in the crystal structure. Residues in the α-helical domain are colored white

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