Premium
Association between the first two immunoglobulin‐like domains of the neural cell adhesion molecule N‐CAM
Author(s) -
Atkins Annette R.,
Osborne Michael J.,
Lashuel Hilal A.,
Edelman Gerald M.,
Wright Peter E.,
Cunningham Bruce A.,
Dyson H.Jane
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00554-2
Subject(s) - antiparallel (mathematics) , immunoglobulin domain , immunoglobulin superfamily , chemistry , fibronectin , covalent bond , molecule , antibody , cell adhesion molecule , extracellular , plasma protein binding , biophysics , cell adhesion , adhesion , binding site , immunoglobulin g , stereochemistry , biochemistry , cell , biology , microbiology and biotechnology , receptor , genetics , physics , organic chemistry , quantum mechanics , magnetic field
The extracellular domain of N‐CAM contains five immunoglobulin‐like (Ig) and two fibronectin type III‐like domains and facilitates cell‐cell binding through multiple, weak interdomain interactions. NMR spectroscopy indicated that the two N‐terminal Ig‐like domains from chicken N‐CAM (Ig I and Ig II) interact with millimolar affinity. Physico‐chemical studies show that this interaction is significantly amplified when the domains are covalently linked, consistent with an antiparallel domain arrangement. The binding of the two individual domains and the dimerization of the concatenated protein were essentially independent of salt, up to a concentration of 200 mM. The residues in Ig I involved in the interaction map to the BED strands of the β sandwich, and delineate a largely hydrophobic patch.