Effect of N-linked glycan density on β-subunit binding for NaV1.4 and NaV1.5. Images show overlapping and superimposed snapshots of glycan conformations from the molecular dynamics simulations, extracted every 5 ns, over a time frame of 150 ns. (A) Top view of NaV1.4, with β1 (magenta), β2 (cyan), and β4 (yellow). (B) Side view of NaV1.4 interacting with β2 and β4. (C) Side view of NaV1.4 interacting with β1. (D) Top view of NaV1.5, with β1, β2, and β4. (E) Side view of NaV1.5 interacting with β2, and β4, assuming the same binding as with NaV1.4. (F) Side view of NaV1.5 interacting with β1, assuming the same binding as with NaV1.4. Glycans are shown in dark gold, with sialylated tips in red.
Figure 5.

Effect of N-linked glycan density on β-subunit binding for Na V 1.4 and Na V 1.5. Images show overlapping and superimposed snapshots of glycan conformations from the molecular dynamics simulations, extracted every 5 ns, over a time frame of 150 ns. (A) Top view of NaV1.4, with β1 (magenta), β2 (cyan), and β4 (yellow). (B) Side view of NaV1.4 interacting with β2 and β4. (C) Side view of NaV1.4 interacting with β1. (D) Top view of NaV1.5, with β1, β2, and β4. (E) Side view of NaV1.5 interacting with β2, and β4, assuming the same binding as with NaV1.4. (F) Side view of NaV1.5 interacting with β1, assuming the same binding as with NaV1.4. Glycans are shown in dark gold, with sialylated tips in red.

This Feature Is Available To Subscribers Only

or Create an Account

Close Modal
Close Modal