Structural highlights
Function
[NCAM2_HUMAN] May play important roles in selective fasciculation and zone-to-zone projection of the primary olfactory axons.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of the first immunoglobulin (Ig1) domain of neural cell adhesion molecule 2 (NCAM2/OCAM/RNCAM) is presented at a resolution of 2.7 A. NCAM2 is a member of the immunoglobulin superfamily of cell adhesion molecules (IgCAMs). In the structure, two Ig domains interact by domain swapping, as the two N-terminal beta-strands are interchanged. beta-Strand swapping at the terminal domain is the accepted mechanism of homophilic interactions amongst the cadherins, another class of CAMs, but it has not been observed within the IgCAM superfamily. Gel-filtration chromatography demonstrated the ability of NCAM2 Ig1 to form dimers in solution. Taken together, these observations suggest that beta-strand swapping could have a role in the molecular mechanism of homophilic binding for NCAM2.
Crystal structure of the Ig1 domain of the neural cell adhesion molecule NCAM2 displays domain swapping.,Rasmussen KK, Kulahin N, Kristensen O, Poulsen JC, Sigurskjold BW, Kastrup JS, Berezin V, Bock E, Walmod PS, Gajhede M J Mol Biol. 2008 Oct 24;382(5):1113-20. Epub 2008 Aug 6. PMID:18706912[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rasmussen KK, Kulahin N, Kristensen O, Poulsen JC, Sigurskjold BW, Kastrup JS, Berezin V, Bock E, Walmod PS, Gajhede M. Crystal structure of the Ig1 domain of the neural cell adhesion molecule NCAM2 displays domain swapping. J Mol Biol. 2008 Oct 24;382(5):1113-20. Epub 2008 Aug 6. PMID:18706912 doi:http://dx.doi.org/10.1016/j.jmb.2008.07.084
