Structure of Human Cytomegalovirus UL141 Binding to TRAIL-R2 Reveals Novel, Non-canonical Death Receptor Interactions
Figure 6
UL141 surface accessibility for receptor binding.
Structure of one UL141 subunit (colored surface) in complex with one TRAIL-R2 (grey cartoon) shown in two views (0° and 180° turn). All three potential N-linked glycosylation sites (Asn117, Asn132 and Asn147) where modeled with a five-sugar Man2GluNac2Fuc glycans, shown in dark grey ball-and-stick). Area A and B indicate available and accessible protein binding sites on UL141, while other available areas are expected to be mostly covered with glycans in the fully glycosylated protein. Location of potential protein-protein binding sites for unbound UL141 were calculated using ProMate (http://bioinfo.weizmann.ac.il/promate). For simplicity, only one UL141 subunit is shown here in molecular surface colored from orange reflecting the lowest probability assigned, to green, assigned to the highest probability. The highest probability areas that reflect possible binding sites in UL141; excluding those binding sites 1–6 of TRAIL-R2 (shown in dotted line here); and are not shield by glycans, are areas A and B.