 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](tz5026fig2mag.jpg)
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Figure 2
Comparison of the crystal packing of (a) the wild-type Keap1 Kelch domain in complex with an Nrf2-derived peptide (PDB entry 2flu; Lo et al., 2006  ), (b) unliganded Keap1 (PDB entry 1zgk; Beamer et al., 2005) and (c) the E540A/E542A double mutant. Residues 540 and 542 in monomers A and B are shown as red and orange spheres, respectively. The access to the Nrf2-binding site is blocked in wild-type Keap1 (b) and free in one of the two protomers of the E540A/E542A double mutant (c). This binding site is occupied by the cyclic peptide. |
![[Figure 2]](tz5026fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
