2OM5

N-Terminal Fragment of Human TAX1

Summary for 2OM5

• Entry DOI: 10.2210/pdb2om5/pdb
• Descriptor: Contactin 2 (1 entity in total)
• Functional Keywords: x-ray crystallography; ig-like c2-type; immunoglobulin superfamily; fibronectin; membrane protein, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor: Q02246
• Total number of polymer chains: 1
• Total formula weight: 42213.49

Authors

Moertl, M.,Sonderegger, P.,Diederichs, K.,Welte, W. (deposition date: 2007-01-20, release date: 2007-11-20, Last modification date: 2024-10-16)

Primary citation

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., 16:2174-2183, 2007

PubMed Abstract: 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.

PubMed: 17766378
DOI: 10.1110/ps.072802707

Experimental method

X-RAY DIFFRACTION (3.07 Å)