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. Author manuscript; available in PMC: 2016 Apr 5.
Published in final edited form as: Chem Res Toxicol. 2008 Aug 26;21(10):2051–2060. doi: 10.1021/tx800226m

Figure 5.

Figure 5

(Panel A) Structures of the Kelch repeat domain after energy minimization. Minimized structure of unmodified Keap1 starting from the coordinates of the crystal structure in the PDB. (Panel B) Minimized structure containing a type 1 disulfide at Cys434, starting from the lowest energy structure of Keap1 docked to noncovalently bound GSH, as described in Experimental Procedures. (Panel C) Minimized structure containing type 1 disulfides at Cys434 and Cys368. In orange are Cys434 and Cys368, the GSH fragment (B and C) is in red, green residues are those that have been shown to contact a peptide fragment of the Neh2 domain of Nrf2 in Keap1-peptide cocrystals, blue is His436, and in mauve are Gly364 and Gly430 (see Discussion).