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. 2015 Nov 20;44(4):1591–1612. doi: 10.1093/nar/gkv1135

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© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 9. — Junction-MoRF in human and yeast Med15 KIX domains. (A) Alignment of yeast Med15-KIX (gray) with human CBP-KIX (green). Yeast KIX structure was generated using PDB id 2K0N. Mutation at VAL-27 (red sphere) reduces the binding affinity of yeast Med15-KIX. VAL-27 aligns with ILE-611 (green sphere) which is the start of G2-loop in human CBP-KIX. (B) Alignment of human Med15-KIX (gray) with human CBP-KIX (green). KIX domain of human Med15 was generated using PDB id 2GUT. Residues ILE-64 (red sphere) and ASP-68 (blue sphere) play a role in maintaining the binding specificity of human Med15-KIX. (C) Alignment of mutated (I64Y and D68K) KIX (wheat) with human KIX (gray) domain. (D) Homology Model of Capsaspora owczarzaki CBP-KIX (yellow) aligned on human CBP-KIX (gray). (E) Homology model of Salpingoeca rosetta CBP-KIX (purple) aligned on Human CBP-KIX (gray). Homology models of C. owczarzaki and S. rosetta CBP-KIX were generated using protein sequences E9CAO3 and F2TVQ2 respectively. Protein sequences were retrieved from UniProt. Human CBP-KIX (gray) was generated using PDB id 2LXT. In all the structures, MoRFs are highlighted in red color, C and N represented C-terminus and N-terminus, respectively.