title: Association between the first two immunoglobulin-like domains of the neural cell adhesion molecule N-CAM.
abstract: 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 beta sandwich, and delineate a largely hydrophobic patch.
authors.affiliation: Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
authors.forename: A R
authors.initials: AR
authors.lastname: Atkins
authors.forename: M J
authors.initials: MJ
authors.lastname: Osborne
authors.forename: H A
authors.initials: HA
authors.lastname: Lashuel
authors.forename: G M
authors.initials: GM
authors.lastname: Edelman
authors.forename: P E
authors.initials: PE
authors.lastname: Wright
authors.forename: B A
authors.initials: BA
authors.lastname: Cunningham
authors.forename: H J
authors.initials: HJ
authors.lastname: Dyson
mesh_terms: D000818:Animals; D002645:Chickens / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D007136:Immunoglobulins / Q000737:chemistry*; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D019006:Neural Cell Adhesion Molecules / Q000737:chemistry*; D011485:Protein Binding
chemical_list: D007136:Immunoglobulins; D019006:Neural Cell Adhesion Molecules