Association between the first two immunoglobulin-like domains of the neural cell adhesion molecule N-CAM

Annette R. Atkins, Michael J. Osborne, Hilal A. Lashuel, Gerald M. Edelman, Peter E. Wright, Bruce A. Cunningham, H. Jane Dyson

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30 Citations (Scopus)

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 β sandwich, and delineate a largely hydrophobic patch. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)162-168
Number of pages7
JournalFEBS Letters
Volume451
Issue number2
DOIs
Publication statusPublished - 21 May 1999
Externally publishedYes

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Keywords

  • Homophilic binding
  • Ig fold
  • N-CAM
  • Nuclear magnetic resonance

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Atkins, A. R., Osborne, M. J., Lashuel, H. A., Edelman, G. M., Wright, P. E., Cunningham, B. A., & Dyson, H. J. (1999). Association between the first two immunoglobulin-like domains of the neural cell adhesion molecule N-CAM. FEBS Letters, 451(2), 162-168. https://doi.org/10.1016/S0014-5793(99)00554-2