7OJ7
Crystal structure of human coxsackievirus A24v in complex with a pentavalent N-acetylneuraminic acid conjugate
This is a non-PDB format compatible entry.
Summary for 7OJ7
| Entry DOI | 10.2210/pdb7oj7/pdb |
| Descriptor | Capsid protein VP1, Capsid protein VP2, Capsid protein VP3, ... (8 entities in total) |
| Functional Keywords | human coxsackievirus a24v, starfish-like inhibitor, corannulene, virus |
| Biological source | Coxsackievirus A24 More |
| Total number of polymer chains | 4 |
| Total formula weight | 98886.35 |
| Authors | Zocher, G.,Stehle, T. (deposition date: 2021-05-14, release date: 2021-10-13, Last modification date: 2024-01-31) |
| Primary citation | Johansson, E.,Caraballo, R.,Hurdiss, D.L.,Mistry, N.,Andersson, C.D.,Thompson, R.F.,Ranson, N.A.,Zocher, G.,Stehle, T.,Arnberg, N.,Elofsson, M. Exploring the Effect of Structure-Based Scaffold Hopping on the Inhibition of Coxsackievirus A24v Transduction by Pentavalent N-Acetylneuraminic Acid Conjugates. Int J Mol Sci, 22:-, 2021 Cited by PubMed Abstract: Coxsackievirus A24 variant (CVA24v) is the primary causative agent of the highly contagious eye infection designated acute hemorrhagic conjunctivitis (AHC). It is solely responsible for two pandemics and several recurring outbreaks of the disease over the last decades, thus affecting millions of individuals throughout the world. To date, no antiviral agents or vaccines are available for combating this disease, and treatment is mainly supportive. CVA24v utilizes Neu5Ac-containing glycans as attachment receptors facilitating entry into host cells. We have previously reported that pentavalent Neu5Ac conjugates based on a glucose-scaffold inhibit CVA24v infection of human corneal epithelial cells. In this study, we report on the design and synthesis of scaffold-replaced pentavalent Neu5Ac conjugates and their effect on CVA24v cell transduction and the use of cryogenic electron microscopy (cryo-EM) to study the binding of these multivalent conjugates to CVA24v. The results presented here provide insights into the development of Neu5Ac-based inhibitors of CVA24v and, most significantly, the first application of cryo-EM to study the binding of a multivalent ligand to a lectin. PubMed: 34445134DOI: 10.3390/ijms22168418 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
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