4MYW
Structure of HSV-2 gD bound to nectin-1
Summary for 4MYW
| Entry DOI | 10.2210/pdb4myw/pdb |
| Related | 3U82 4MYV |
| Descriptor | Envelope glycoprotein D, Poliovirus receptor-related protein 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
| Functional Keywords | igv-like core, n-/c-terminal extensions, tandem arranged v-c-c ig-like domains, receptor binding, cell surface attachment, viral, cellular surface, viral protein-cell adhesion complex, viral protein/cell adhesion |
| Biological source | Human herpesvirus 2 (HHV-2) More |
| Total number of polymer chains | 4 |
| Total formula weight | 141157.13 |
| Authors | |
| Primary citation | Lu, G.,Zhang, N.,Qi, J.,Li, Y.,Chen, Z.,Zheng, C.,Gao, G.F.,Yan, J. Crystal structure of herpes simplex virus 2 gD bound to nectin-1 reveals a conserved mode of receptor recognition. J.Virol., 88:13678-13688, 2014 Cited by PubMed Abstract: Herpes simplex virus 1 (HSV-1) and HSV-2 are among the most prevalent human pathogens. Both viruses can recognize, via the surface envelope glycoprotein D (gD), human nectin-1 as a functional receptor. Previous studies have successfully elucidated the molecular basis of the binding between HSV-1 gD and nectin-1 by cocrystallography. Despite a high sequence identity between HSV-1 and HSV-2 gDs, the atomic intermolecule details for the HSV-2-gD/nectin-1 interaction remain elusive. Here, we report the crystal structures of both the unbound and the nectin-1-bound HSV-2 gDs. The free-gD structure expectedly comprises an IgV-like core and the surface-exposed terminal extensions as observed in its HSV-1 counterpart but lacks traceable electron densities for a large portion of the terminal elements. These terminal residues were clearly traced in the complex structure as a definitive loop in the N terminus and an α-helix in the C terminus, thereby showing a conserved nectin-1-binding mode as reported for HSV-1 gD. The interface residues in nectin-1 were further mutated and tested for the gD interaction by surface plasmon resonance. The resultant binding patterns were similar for HSV-1 and HSV-2 gDs, further supporting a homologous receptor-binding basis by the two viruses for nectin-1. These data, together with a cell-based fusion assay showing a cross-inhibition of the gD/nectin-1-mediated cell-cell fusion by soluble HSV-1 and HSV-2 gDs, provided solid structural and functional evidence that HSV-1 and HSV-2 recognize nectin-1 via the same binding mode. Finally, we also demonstrated that nectin-1 I80 is an important residue involved in gD interaction. PubMed: 25231300DOI: 10.1128/JVI.01906-14 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.189 Å) |
Structure validation
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