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. 2012 Jun 18;13(6):7532–7549. doi: 10.3390/ijms13067532

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© 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.

This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Docking simulation. (A) Residues forming Pocket 3 and its vicinity are shown by surface representation in gray except for F148 in light green and L52 in yellow. The type 2 motif peptide is represented by a stick model in which atoms of carbon, nitrogen and oxygen are shown in cyan, blue and red, respectively, in the upper panel. A side view of the structure shown in the upper panel obtained by rotating 60° around the indicated axis is presented in the lower panel; (B) The peptide shown in (A) upper panel is rotated 75° around the axis and represented in stereoview (parallel viewing method). Hydrophobic interactions between the type 2 motif peptide and ALG-2 are shown for F148 (carbon atoms, green) and L52 (carbon atoms, yellow). Broken lines indicate hydrophobic interactions with distances shorter than or equal to 3.9 Å (see Table 3 for details).