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Structure of the N‐terminal dimerization domain of CEACAM7
Author(s) -
Bonsor Daniel A.,
Beckett Dorothy,
Sundberg Eric J.
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15013576
Subject(s) - terminal (telecommunication) , chemistry , adhesion , affinities , sedimentation equilibrium , cell adhesion , hydrogen bond , c terminus , biophysics , domain (mathematical analysis) , stereochemistry , crystallography , cell , molecule , biochemistry , biology , enzyme , amino acid , telecommunications , mathematical analysis , mathematics , organic chemistry , computer science
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. It achieves cell adhesion through dimerization of the N‐terminal IgV domain. The crystal structure of the N‐terminal dimerization domain of CEACAM has been determined at 1.47 Å resolution. 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 K dimerization for CEACAM7 determined by sedimentation equilibrium is tenfold tighter than that measured for CEACAM5. These findings suggest that the dimerization affinities of CEACAMs are modulated via sequence variation in the dimerization surface.