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. 2016 Nov 3;6:36366. doi: 10.1038/srep36366

Figure 1. HUSpm dimer.

Figure 1

(a) Ribbon structure of the HUSpm dimer coloured by the canonical domain structure: the HTH domain in red, the DBD domain in green, and the DS region in blue (see comments in the text). The N- and C-termini for one subunit are indicated. One monomer is coloured in grey for clarity. (b) The residues involved in the formation of the hydrophobic core of the HUSpm dimer are shown in blue and cyan for two monomers, respectively. The orientation of the molecule is the same as in (а). The non-conserved Phe14, Phe29, and Val17 residues of both monomers are in magenta. For the reasons of clarity, the ribbon model of the dimer is semitransparent.