6LS9
Crystal structure of bovine herpesvirus 1 glycoprotein D
Summary for 6LS9
| Entry DOI | 10.2210/pdb6ls9/pdb |
| Related PRD ID | PRD_900017 |
| Descriptor | Envelope glycoprotein D, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | receptor recognition, viral protein |
| Biological source | Bovine alphaherpesvirus 1 |
| Total number of polymer chains | 3 |
| Total formula weight | 105906.12 |
| Authors | Yue, D.,Chen, Z.J.,Yang, F.L.,Ye, F.,Lin, S.,Cheng, Y.W.,Wang, J.C.,Chen, Z.M.,Lin, X.,Yang, J.,Chen, H.,Zhang, Z.L.,You, Y.,Sun, H.L.,Wen, A.,Wang, L.L.,Zheng, Y.,Cao, Y.,Li, Y.H.,Lu, G.W. (deposition date: 2020-01-17, release date: 2020-06-17, Last modification date: 2024-10-30) |
| Primary citation | Yue, D.,Chen, Z.,Yang, F.,Ye, F.,Lin, S.,He, B.,Cheng, Y.,Wang, J.,Chen, Z.,Lin, X.,Yang, J.,Chen, H.,Zhang, Z.,You, Y.,Sun, H.,Wen, A.,Wang, L.,Zheng, Y.,Cao, Y.,Li, Y.,Lu, G. Crystal structure of bovine herpesvirus 1 glycoprotein D bound to nectin-1 reveals the basis for its low-affinity binding to the receptor. Sci Adv, 6:eaba5147-eaba5147, 2020 Cited by PubMed Abstract: Bovine herpesvirus 1 (BHV-1) has received increasing attention for its potential oncolytic applications. BHV-1 recognizes nectin-1 for cell entry via viral glycoprotein D (gD) but represents a low-affinity nectin-1 binding virus. The molecular basis underlying this low receptor-binding affinity, however, remains unknown. Here, the crystal structures of BHV-1 gD in the free and nectin-1-bound forms are presented. While showing an overall resembled nectin-1 binding mode to other alphaherpesvirus gDs, BHV-1 gD has a unique G-strand/α2-helix interloop that disturbs gD/nectin-1 interactions. Residue R188 residing in this loop is observed to otherwise cause strong steric hindrance with the bound receptor, making a large conformational change of the loop a prerequisite for nectin-1 engagement. Subsequently, substitution of R188 with glycine markedly enhances the affinity of the BHV-1-gD/nectin-1 interaction (by about fivefold). These structural and functional data delineate the receptor-recognition basis for BHV-1, which might facilitate BHV-1-based oncolytic design in the future. PubMed: 32426511DOI: 10.1126/sciadv.aba5147 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.503 Å) |
Structure validation
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