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. 2013 Oct 15;14(10):20578–20596. doi: 10.3390/ijms141020578

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© 2013 by the authors; licensee MDPI, 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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Lipophilic potential of the ligand-binding sites of the QS LuxR and of the prototype of the PAB LuxR solos subfamily. (a) TraR (PDB_ID 1H0M [24]) in light pink (showing the side chains of the conserved core in yellow, of the specificity patch in magenta and of the variable patch in orange); (b) SdiA (PDB_ID 2AVX [30]) in light blue; (c) LasR (PDB_ID 3IX3) in light orange; (d) CviR (PDB_ID 3QP1 [29]) in light green; (e) QscR (PDB_ID 3SZT [28]) in light yellow; (f) OryR model in blue purple. The hydrophobic surface is indicated by yellow and the hydrophilic surface by cyan. Left column: top view (same orientation of the previous Figures); Right column: bottom view (obtained by 180 degrees rotation around y axis). Figures produced by Pymol [33].

Lipophilic potential of the ligand-binding sites of the QS LuxR and of the prototype of the PAB LuxR solos subfamily. (a) TraR (PDB_ID 1H0M [24]) in light pink (showing the side chains of the conserved core in yellow, of the specificity patch in magenta and of the variable patch in orange); (b) SdiA (PDB_ID 2AVX [30]) in light blue; (c) LasR (PDB_ID 3IX3) in light orange; (d) CviR (PDB_ID 3QP1 [29]) in light green; (e) QscR (PDB_ID 3SZT [28]) in light yellow; (f) OryR model in blue purple. The hydrophobic surface is indicated by yellow and the hydrophilic surface by cyan. Left column: top view (same orientation of the previous Figures); Right column: bottom view (obtained by 180 degrees rotation around y axis). Figures produced by Pymol [33].