id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-002395-goil7gjr	dos Santos, Ália	Oligomerization domains in the glycan‐binding receptors DC‐SIGN and DC‐SIGNR: Sequence variation and stability differences	2016-12-22		.txt	text/plain	5638	228	49	The results demonstrate that two features characterize repeat units which form more stable tetramers: a leucine reside in the first position of the heptad pattern of hydrophobic residues that pack on the inside of the coiled coil and an arginine residue on the surface of the coiled coil that forms a salt bridge with a glutamic acid residue in the same polypeptide chain. Gel filtration revealed that this version of the neck domain forms a stable tetramer at room temperature since it elutes at the same position as a natural fragment of the neck domain of DC-SIGNR containing seven repeat units, which has been characterized as a tetramer [ Fig. 3(A) ]. The studies reported here suggest that the presence of stabilizing residues at positions 6 and 15 of the repeat units allows for the formation of stable tetramers even for shorter versions of the neck domain present in some individuals, which result from common genetic polymorphisms in the human population.	./cache/cord-002395-goil7gjr.txt	./txt/cord-002395-goil7gjr.txt