Structural highlights
Function
[CNTN2_HUMAN] May play a role in the initial growth and guidance of axons. May be involved in cell adhesion.
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
Human TAG-1 is a neural cell adhesion molecule that is crucial for the development of the nervous system during embryogenesis. It consists of six immunoglobulin-like and four fibronectin III-like domains and is anchored to the membrane by glycosylphosphatidylinositol. Herein we present the crystal structure of the four N-terminal immunoglobulin-like domains of TAG-1 (TAG-1(Ig1-4)), known to be important in heterophilic and homophilic macromolecular interactions. The contacts of neighboring molecules within the crystal were investigated. A comparison with the structure of the chicken ortholog resulted in an alternative mode for the molecular mechanism of homophilic TAG-1 interaction. This mode of TAG-1 homophilic interaction is based on dimer formation rather than formation of a molecular zipper as proposed for the chicken ortholog.
The crystal structure of the ligand-binding module of human TAG-1 suggests a new mode of homophilic interaction.,Mortl M, Sonderegger P, Diederichs K, Welte W Protein Sci. 2007 Oct;16(10):2174-83. Epub 2007 Aug 31. PMID:17766378[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mortl M, Sonderegger P, Diederichs K, Welte W. The crystal structure of the ligand-binding module of human TAG-1 suggests a new mode of homophilic interaction. Protein Sci. 2007 Oct;16(10):2174-83. Epub 2007 Aug 31. PMID:17766378 doi:10.1110/ps.072802707
