2OM5

N-Terminal Fragment of Human TAX1

2OM5 の概要

• エントリーDOI: 10.2210/pdb2om5/pdb
• 分子名称: Contactin 2 (1 entity in total)
• 機能のキーワード: x-ray crystallography; ig-like c2-type; immunoglobulin superfamily; fibronectin; membrane protein, cell adhesion
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Lipid-anchor, GPI-anchor: Q02246
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42213.49

構造登録者

Moertl, M.,Sonderegger, P.,Diederichs, K.,Welte, W. (登録日: 2007-01-20, 公開日: 2007-11-20, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.07 Å)