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Figure 8
Experimentally determined crystal structure of GG-353. (a) Square channels formed down the c axis of the crystal structure, with channel formation facilitated by hydrogen-bonding interactions between terminal residues. Positions of attachment of the flexible fatty-acid conjugate molecule onto Lys17 are indicated with red arrows; positions of attachment of flexible amidated C-terminal residues are indicated with black arrows. (b) Pore formation is facilitated by stacking of the helical peptide portions to form clockwise-ascending spirals. GG-353 monomers are coloured by crystal symmetry. (c) Hydrophobicity of a GG-353 molecule superimposed into the crystal packing, with hydrophobic regions (beige) buried within the crystal structure and hydrophilic regions (blue) exposed to solvent channels. (d) C⋯H—π interactions around Phe22 (with Ile23, Leu26 and Ile27) forming the primary crystal contact between square motifs in the lattice.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 82| Part 4| April 2026| Pages 114-124
https://doi.org/10.1107/S2053230X26001937
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