Extended Data Fig. 6: Electrostatic surface potential and glycosylation of the HCMV gH/UL116/UL141 GATE. | Nature Microbiology

Extended Data Fig. 6: Electrostatic surface potential and glycosylation of the HCMV gH/UL116/UL141 GATE.

From: The GATE glycoprotein complex enhances human cytomegalovirus entry in endothelial cells

Extended Data Fig. 6: Electrostatic surface potential and glycosylation of the HCMV gH/UL116/UL141 GATE.The alternative text for this image may have been generated using AI.

a, Electrostatic surface potential of the HCMV GATE complex displayed on a space-filling model, with positively charged regions in blue and negatively charged regions in red. The negatively charged cleft is outlined. Electrostatic potential maps were generated using the PDB2PQR and APBS software. b, Side and top views of the glycosylation site distribution on the HCMV gH/UL116/UL141 GATE complex. c, Inset showing the glycosylation site distribution at the gH-UL116 interaction site, as resolved in the symmetry-expanded focused refinement of the gH-UL116 interface.

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