id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-255841-3laov764	Duquerroy, Stéphane	Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein()	2005-05-10		.txt	text/plain	6758	315	62	A striking arrangement of conserved asparagine and glutamine residues of HR1 propagates from two central chloride ions, providing hydrogen-bonding "zippers" that strongly constrain the path of the HR2 main chain, forcing it to adopt an extended conformation at either end of a short HR2 α-helix. We and others have previously shown that, analogous to other class I fusion proteins, peptides corresponding to the HR regions of the mouse hepatitis coronavirus (MHV, Bosch et al., 2003) and SARS-CoV (Bosch et al., 2004; Ingallinella et al., 2004; Xu et al., 2004a; Tripet et al., 2004) can fold into a stable rod-like structure, consisting of three HR1 helices in association with three HR2 peptides in antiparallel orientation. As expected, there is essentially one side chain per turn of the HR1 a-helix participating to the central hydrophobic core of the molecule, resulting in 23 amino acids from each chain (labeled to the left of Fig. 2A ) interacting with their symmetry mates at the central 3-fold axis.	./cache/cord-255841-3laov764.txt	./txt/cord-255841-3laov764.txt