3Q2W

Crystal structure of mouse N-cadherin ectodomain

3Q2W の概要

• エントリーDOI: 10.2210/pdb3q2w/pdb
• 関連するPDBエントリー: 3Q2V
• 分子名称: Cadherin-2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: cadherin, cell adhesion, calcium binding
• 由来する生物種: Mus musculus (mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 65144.47

構造登録者

Jin, X.,Shapiro, L. (登録日: 2010-12-20, 公開日: 2011-02-23, 最終更新日: 2024-10-30)

主引用文献

Harrison, O.J.,Jin, X.,Hong, S.,Bahna, F.,Ahlsen, G.,Brasch, J.,Wu, Y.,Vendome, J.,Felsovalyi, K.,Hampton, C.M.,Troyanovsky, R.B.,Ben-Shaul, A.,Frank, J.,Troyanovsky, S.M.,Shapiro, L.,Honig, B.
The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins.
Structure, 19:244-256, 2011

PubMed Abstract: Adherens junctions, which play a central role in intercellular adhesion, comprise clusters of type I classical cadherins that bind via extracellular domains extended from opposing cell surfaces. We show that a molecular layer seen in crystal structures of E- and N-cadherin ectodomains reported here and in a previous C-cadherin structure corresponds to the extracellular architecture of adherens junctions. In all three ectodomain crystals, cadherins dimerize through a trans adhesive interface and are connected by a second, cis, interface. Assemblies formed by E-cadherin ectodomains coated on liposomes also appear to adopt this structure. Fluorescent imaging of junctions formed from wild-type and mutant E-cadherins in cultured cells confirm conclusions derived from structural evidence. Mutations that interfere with the trans interface ablate adhesion, whereas cis interface mutations disrupt stable junction formation. Our observations are consistent with a model for junction assembly involving strong trans and weak cis interactions localized in the ectodomain.

PubMed: 21300292
DOI: 10.1016/j.str.2010.11.016

実験手法

X-RAY DIFFRACTION (3.2 Å)