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. 2013 Aug 27;8(8):e71512. doi: 10.1371/journal.pone.0071512

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© 2013 Guellouz 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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(A) Ribbon representation of the two bNCS-16/NCS-3.24 complexes present in the asymmetric unit. (B) Comparison of the NCS-3.24/testosterone complex (NCS-3.24 is in grey and testosterone hemisuccinate are in blue) with the bNCS-16/NCS-3.24 complex (same colour code as panel A). For clarity, only loops from NCS-3.24 that undergo conformational changes are shown.(C) Representation of the interface between bNCS-16 and NCS-3.24 (same colour code as panel A). Residues involved in the interaction are shown as sticks. Residues from the interface, which belong to the invariant scaffold of αRep proteins are shown as ball and sticks. Hydrogen bonds are depicted by dashed lines.