Fig. 3: Molecular modeling of PF4-heparin interaction. | Communications Biology

Fig. 3: Molecular modeling of PF4-heparin interaction.

From: Molecular architecture and platelet-activating properties of small immune complexes assembled on heparin and platelet factor 4

Fig. 3

Representative structures of dp40·PF4 (A), dp70·PF4 (B) and dp100·PF4 (C) complexes produced by molecular modeling (yielding 1:1, 1:2 and 1:3 heparin/PF4 complexes, respectively). The iso-potential surfaces (A: 5.5 kT/e and B, C: 7.5kT/e) represent the positive belts around the protein, while the heparin chain is shown using a space-fill model (without a corresponding iso-potential surface). In all three cases the initial conformation of heparin was an extended chain; the complete wrapping of the heparin chain around the PF4 tetramers and formation of the compact structures took up to 200 ns of simulation time (see Figure S3 in Supplementary Material for details of the molecular modeling work and the convergence/reproducibility of simulations).

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