Figure 2
From: SOXE neofunctionalization and elaboration of the neural crest during chordate evolution
HMG Structure and sequence alignment of SOXE proteins.
(a) Sequence alignment of SOXE proteins. Invariant residues are shaded black, conserved residues gray and variable residues white. The DIM and the HMG are boxed. The arrows indicate the sites with potential effects on dimerization some of which were interrogated experimentally28. (b) Structural model of a SOXE dimer on a palindromic DNA sequence with 5bp spacer. Models were prepared as described in Palasingam et al.56 using structural coordinates from protein data bank entry 3f27 as template (http://www.sciencedirect.com/science/article/pii/S0022283609003635). DNA is shown as gray surface and the HMG boxes of two juxtaposed SOXE molecules as black cartoon. Residues varying amongst HMG boxes of SOXE proteins are shown as ball-and-stick. The DIM domains of unknown structure are schematically depicted with dotted lines.
