How does binding of imidazole-based inhibitors to heme oxygenase-1 influence their conformation? Insights combining crystal structures and molecular modelling

Carletta, A.; Tilborg, A.; Moineaux, L.; de Ruyck, J.; Basile, L.; Salerno, L.; Romeo, G.; Wouters, J.; Guccione, S.

doi:10.1107/S2052520615010410

Acta Crystallographica Section B
Acta Crystallographica
Section B STRUCTURAL SCIENCE, CRYSTAL ENGINEERING AND MATERIALS

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Figure 3
Ribbon representation of the human HO-1 enzyme (3k4f ) highlighting the active site with the heme group and ligand (1a) (a); docking binding modes for compounds (1a) and (1b) (b) and for (1c) and (2a) (c). Reduction of the carbonyl group on the ethylene spacer [(1c) versus (2aS)] leads to a small decrease of the HO-1 inhibition for the (para)-nitro derivatives. We speculate that the second binding mode is less probable and that, after induced fit, the nitro analogues could lead to the first most probable binding mode, observed in the protein crystal structures.

STRUCTURAL SCIENCE
CRYSTAL ENGINEERING
MATERIALS

ISSN: 2052-5206

Volume 71| Part 4| July 2015| Pages 447-454

doi:10.1107/S2052520615010410

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