id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-312946-p2iazl7z	Ziółkowska, Natasza E.	Domain-Swapped Structure of the Potent Antiviral Protein Griffithsin and Its Mode of Carbohydrate Binding	2006-07-18		.txt	text/plain	6939	306	54	The crystal structure of griffithsin, an antiviral lectin from the red alga Griffithsia sp., was solved and refined at 1.3 Å resolution for the free protein and 0.94 Å for a complex with mannose. Antiviral potency of griffithsin is likely due to the presence of multiple, similar sugar binding sites that provide redundant attachment points for complex carbohydrate molecules present on viral envelopes. Another conserved broad loop with the GGSGG sequence, 86-90, is located near the secondary carbohydrate binding site in calsepa and follows a course quite different than in banana and parkia lectins, yet similar to the path in the other proteins. The second crystal form, grown from material expressed in plants and containing only 121 residues in a protein chain, was orthorhombic (P2 1 2 1 2 1 ) and contained two griffithsin molecules in the asymmetric unit.	./cache/cord-312946-p2iazl7z.txt	./txt/cord-312946-p2iazl7z.txt