Structure and interactions of NCAM modules 1 and 2, basic elements in neural cell adhesion

Citation
Ph. Jensen et al., Structure and interactions of NCAM modules 1 and 2, basic elements in neural cell adhesion, NAT ST BIOL, 6(5), 1999, pp. 486-493
Citations number
28
Categorie Soggetti
Biochemistry & Biophysics
Journal title
NATURE STRUCTURAL BIOLOGY
ISSN journal
10728368 → ACNP
Volume
6
Issue
5
Year of publication
1999
Pages
486 - 493
Database
ISI
SICI code
1072-8368(199905)6:5<486:SAIONM>2.0.ZU;2-T
Abstract
The structure in solution of the second Ig-module fragment of residues 117- 208 of NCAM has been determined. Like the first Ig-module of residues 20-11 6, it belongs to the I set of the immunogloblin superfamily. Module 1 and m odule 2 interact weakly, and the binding sites of this interaction have bee n identified. The two-module fragment NCAM(20-208) is a stable dimer, Remov al of the charged residues in these sites in NCAM(20-208) abolishes the dim erization. Modeling the dimer of NCAM(20-208) to fit the interactions of th ese charges produces one coherent binding site for the formation of two ant iparallel strands of the first two NCAM modules. This mode of binding could be a major element in trans-cellular interactions in neural cell adhesion.