id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-255350-dmbl4emn	Bonsor, Daniel A.	Structure of the N-terminal dimerization domain of CEACAM7	2015-08-25		.txt	text/plain	2790	171	68	CEACAM7 is a human cellular adhesion protein that is expressed on the surface of colon and rectum epithelial cells and is downregulated in colorectal cancers. The overall fold of CEACAM7 is similar to those of CEACAM1 and CEACAM5; however, there are differences, the most notable of which is an insertion that causes the C′′ strand to buckle, leading to the creation of a hydrogen bond in the dimerization interface. The dimer interface is formed from the second -sheet, A 0 GFCC 0 C 00 , specifically the GFCC 0 C 00 strands and the CC 0 , C 0 C 00 and FG loops (Fig. 1c) . The dimerization constant of CEACAM7 was estimated by sedimentation-equilibrium analysis using analytical ultrain 50 mM Tris-HCl, 50 mM sodium chloride pH 7.5 with rotor speeds of 29 000, 32 000 and 35 000 rev min À1 (blue, red and green curves, respectively).	./cache/cord-255350-dmbl4emn.txt	./txt/cord-255350-dmbl4emn.txt