Figure 2.
(A) The membrane disruption complex formed in a carpet-like model of membrane disruption by NaD1 (PDB: 6B55) engaging PA (three dimer pairs shown in aqua, four dimer pairs shown in gold). (B) The conserved cationic grip of an NaD1 dimer (PDB: 4CQK) (monomer 1 in cyan, monomer 2 in pink) binding two PI(4,5)P2 molecules (grey and black). (C) The oligomer of NsD7–PA (PDB: 5KK4) showing the NsD7 double helix (helix 1 in blue, helix 2 in red). PA (yellow) is bound in between the dimers and in the cationic grip. (D) Comparison of NsD7 (PDB: 5VYP) (green) and NaD1 (PDB: 4CQK) (blue) engaging PI(4,5)P2 (orange for NaD1, yellow for NsD7), both of which form multimeric arch-shaped oligomers that are proposed to exert torsional strain on the membrane. (E) The asymmetric dimer of HBD-2 (PDB: 6CS9) (monomer 1 in salmon, monomer 2 in orange) showing the two PI(4,5)P2 binding sites (lipids shown in grey and black). Images generated using PyMOL.
X-ray crystal structures of defensin–lipid complexes.

(A) The membrane disruption complex formed in a carpet-like model of membrane disruption by NaD1 (PDB: 6B55) engaging PA (three dimer pairs shown in aqua, four dimer pairs shown in gold). (B) The conserved cationic grip of an NaD1 dimer (PDB: 4CQK) (monomer 1 in cyan, monomer 2 in pink) binding two PI(4,5)P2 molecules (grey and black). (C) The oligomer of NsD7–PA (PDB: 5KK4) showing the NsD7 double helix (helix 1 in blue, helix 2 in red). PA (yellow) is bound in between the dimers and in the cationic grip. (D) Comparison of NsD7 (PDB: 5VYP) (green) and NaD1 (PDB: 4CQK) (blue) engaging PI(4,5)P2 (orange for NaD1, yellow for NsD7), both of which form multimeric arch-shaped oligomers that are proposed to exert torsional strain on the membrane. (E) The asymmetric dimer of HBD-2 (PDB: 6CS9) (monomer 1 in salmon, monomer 2 in orange) showing the two PI(4,5)P2 binding sites (lipids shown in grey and black). Images generated using PyMOL.

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