Figure 1

Figure 1. Structure of HIP14 ankyrin repeats. From: The ankyrin repeat domain of Huntingtin interacting protein 14 contains a surface aromatic cage, a potential site for methyl-lysine binding.

(A) Superimposition of molecule A (green) and C (magenta), two of the three molecules in the crystallographic asymmetric unit. Molecule A contains an intact N-terminus, but the last seven residues (282-288) are disordered; while the first eight (51-58) and the last four residues (285-288) are disordered in molecule C. In molecule B (not shown), the first two (51-52) and the last nine residues (280-288) are disordered.
(B) Superimposition of HIP14 ankyrin repeats (molecule C) and GLP ankyrin repeats (blue; PDB 3B95). Sequence conservation between the two proteins is scattered throughout of ANK2 to ANK7 (Table 3). It is possible that either protein could have an additional repeat either extended in the N-terminus (GLP) or in the C-terminus (HIP14). The histone H3 peptide bound with GLP is shown in stick model (yellow) with blue for nitrogen and red for oxygen atoms.
(C) Close-up view of the cages (magenta for HIP14 and blue for GLP) formed by the residues of ANK4 and ANK5. The di-methylated lysine (yellow) is inserted into the partial hydrophobic cage of GLP. A tri-methylated lysine could be inserted into the all-hydrophobic cage of HIP14.

Tiyu Gao, et al. Proteins. ;76(3):772-777.

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