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. 2015 Dec 21;11(12):e1004659. doi: 10.1371/journal.pcbi.1004659

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© 2015 Parra et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Fig 8 — Quaternary assemblies that involve ANKs are shown with the ANK molecule in orange and the rest of the complex in yellow. Residues from the ANK structure that are involved at the interface are coloured in magenta. A) Myosin phosphatase targeting subunit 1 (MYPT1) in complex with the ser/thr phosphatase-1 (delta) (PdbID: 1s70). B) IκBβ/NF-κB p65 homodimer complex (PdbID: 1k3z) C) YAR1 when binding the 40S ribosomal protein S3 (PdbID: 4bsz) D) Tankyrase-1, (PdbID: 3utm). E) Change in the configurational frustration index between the unbound and bound states for the ANK proteins. In the x-axis the configurational frustration for the monomeric unbound state is shown. In the y-axis the difference between the complexed state and the monomeric state is shown. A positive change means that the frustration is decreased upon interaction.