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. Author manuscript; available in PMC: 2011 Apr 13.
Published in final edited form as: Biochemistry. 2010 Apr 13;49(14):3101–3115. doi: 10.1021/bi902183w

Figure 8.

Figure 8

α-Cyclodextrins are shown acting as hosts to various side chains within their cavities. Key platform-forming aromatic residues are also highlighted. (a) α-Cyclodextrin ring I bridges between 21 screw related molecules. Asn53 is the guest side chain; Tyr276 and Trp284 of the symmetry related molecule (in magenta) are the platform residues. (b) α-Cyclodextrin ring II is in the active site cleft. Val163 is the guest side chain for this ring. Trp59 at the bottom of the active site cleft is the platform residue. (c) Trp134 is the guest side chain for α-cyclodextrin ring III. Tyr174 is the platform residue.