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. 2012 Nov 13;7(11):e49195. doi: 10.1371/journal.pone.0049195

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© 2012 Helbling 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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-T (left panels (A, and C)) and WT -T (right panels (B, and D)). Top panels (A, B): the van der Waals space occupied by residues in the binding pocket is highlighted by the wireframe representation. The different conformation of the hydrophobic tail in -T and -T is evidenced. Lower panels (C, D): comparison between the interaction of -T (C) and -T with the helical mobile gate of the WT protein.

Inline graphic — -T (left panels (A, and C)) and WT -T (right panels (B, and D)). Top panels (A, B): the van der Waals space occupied by residues in the binding pocket is highlighted by the wireframe representation. The different conformation of the hydrophobic tail in -T and -T is evidenced. Lower panels (C, D): comparison between the interaction of -T (C) and -T with the helical mobile gate of the WT protein.