3NCM
NEURAL CELL ADHESION MOLECULE, MODULE 2, NMR, 20 STRUCTURES
Summary for 3NCM
| Entry DOI | 10.2210/pdb3ncm/pdb |
| Descriptor | PROTEIN (NEURAL CELL ADHESION MOLECULE, LARGE ISOFORM) (1 entity in total) |
| Functional Keywords | cell adhesion, glycoprotein, heparin-binding, gpi-anchor, neural adhesion molecule, immunoglobulin fold, homophilic binding, cell adhesion protein |
| Biological source | Rattus norvegicus (Norway rat) |
| Total number of polymer chains | 1 |
| Total formula weight | 10581.34 |
| Authors | Jensen, P.H.,Soroka, V.,Thomsen, N.K.,Berezin, V.,Bock, E.,Poulsen, F.M. (deposition date: 1998-09-21, release date: 1999-07-23, Last modification date: 2024-11-06) |
| Primary citation | Jensen, P.H.,Soroka, V.,Thomsen, N.K.,Ralets, I.,Berezin, V.,Bock, E.,Poulsen, F.M. Structure and interactions of NCAM modules 1 and 2, basic elements in neural cell adhesion Nat.Struct.Biol., 6:486-493, 1999 Cited by PubMed 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 20-116, it belongs to the I set of the immunogloblin superfamily. Module 1 and module 2 interact weakly, and the binding sites of this interaction have been identified. The two-module fragment NCAM(20-208) is a stable dimer. Removal of the charged residues in these sites in NCAM(20-208) abolishes the dimerization. Modeling the dimer of NCAM(20-208) to fit the interactions of these charges produces one coherent binding site for the formation of two antiparallel strands of the first two NCAM modules. This mode of binding could be a major element in trans-cellular interactions in neural cell adhesion. PubMed: 10331878DOI: 10.1038/8292 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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