3LNG

Crystal structure of E-cadherin EC12 AA extension

3LNG の概要

• エントリーDOI: 10.2210/pdb3lng/pdb
• 関連するPDBエントリー: 3LND 3LNE 3LNF 3LNH 3LNI
• 分子名称: Cadherin-1, CALCIUM ION (3 entities in total)
• 機能のキーワード: cadherin, calcium, cell adhesion, cell junction, cell membrane, cleavage on pair of basic residues, glycoprotein, membrane, transmembrane
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Cell junction: P09803
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47046.51

構造登録者

Harrison, O.,Jin, X.,Shapiro, L. (登録日: 2010-02-02, 公開日: 2010-03-02, 最終更新日: 2023-09-06)

主引用文献

Harrison, O.J.,Bahna, F.,Katsamba, P.S.,Jin, X.,Brasch, J.,Vendome, J.,Ahlsen, G.,Carroll, K.J.,Price, S.R.,Honig, B.,Shapiro, L.
Two-step adhesive binding by classical cadherins.
Nat.Struct.Mol.Biol., 17:348-357, 2010

PubMed Abstract: Crystal structures of classical cadherins have revealed two dimeric configurations. In the first, N-terminal beta-strands of EC1 domains 'swap' between partner molecules. The second configuration (the 'X dimer'), also observed for T-cadherin, is mediated by residues near the EC1-EC2 calcium binding sites, and N-terminal beta-strands of partner EC1 domains, though held adjacent, do not swap. Here we show that strand-swapping mutants of type I and II classical cadherins form X dimers. Mutant cadherins impaired for X-dimer formation show no binding in short-time frame surface plasmon resonance assays, but in long-time frame experiments, they have homophilic binding affinities close to that of wild type. Further experiments show that exchange between monomers and dimers is slowed in these mutants. These results reconcile apparently disparate results from prior structural studies and suggest that X dimers are binding intermediates that facilitate the formation of strand-swapped dimers.

PubMed: 20190754
DOI: 10.1038/nsmb.1784

実験手法

X-RAY DIFFRACTION (2.7 Å)