id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-332165-31tbc31x	Rustmeier, Nils H.	The Symmetry of Viral Sialic Acid Binding Sites—Implications for Antiviral Strategies	2019-10-14		.txt	text/plain	5820	316	43	In this review, we will evaluate the structures of non-enveloped virus capsid proteins bound to sialylated glycan receptors and discuss the potential of these structures for the development of potent antiviral attachment inhibitors. This concept of targeting multiple, symmetric receptor binding sites by multivalent inhibitors is also applicable for many viruses, since viral capsids are often icosahedral and, therefore, highly symmetric structures. Many members of the polyomavirus family bind sialic acid-based glycans using their VP1 proteins, so the binding sites on individual pentamers are always linked by local five-fold symmetry (Figure 4a , TSPyV). The glycooligopeptide-VP1 complex structures displayed a similar ligand binding mode that was reported for sialic acid in an earlier study [50] and showed, for the compounds, that the linker between the ligand and the scaffold occupies the space that is usually targeted by the natural glycan receptor moieties (Figure 5a,b, right) .	./cache/cord-332165-31tbc31x.txt	./txt/cord-332165-31tbc31x.txt