1L3W

C-cadherin Ectodomain

1L3W の概要

• エントリーDOI: 10.2210/pdb1l3w/pdb
• 関連するPDBエントリー: 1EDH 1FF5 1NCG 1NCH 1NCI
• 分子名称: EP-cadherin, 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-alpha-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: cell adhesion, calcium binding, cadherin, extracellular, ectodomain, metal binding protein
• 由来する生物種: Xenopus laevis (African clawed frog)
• 細胞内の位置: Cell membrane; Single-pass type I membrane protein: P33148
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 64205.15

構造登録者

Boggon, T.J.,Murray, J.,Chappuis-Flament, S.,Wong, E.,Gumbiner, B.M.,Shapiro, L. (登録日: 2002-03-01, 公開日: 2002-04-26, 最終更新日: 2023-08-16)

主引用文献

Boggon, T.J.,Murray, J.,Chappuis-Flament, S.,Wong, E.,Gumbiner, B.M.,Shapiro, L.
C-cadherin ectodomain structure and implications for cell adhesion mechanisms
Science, 296:1308-1313, 2002

PubMed Abstract: Cadherins are transmembrane proteins that mediate adhesion between cells in the solid tissues of animals. Here we present the 3.1 angstrom resolution crystal structure of the whole, functional extracellular domain from C-cadherin, a representative "classical" cadherin. The structure suggests a molecular mechanism for adhesion between cells by classical cadherins, and it provides a new framework for understanding both cis (same cell) and trans (juxtaposed cell) cadherin interactions. The trans adhesive interface is a twofold symmetric interaction defined by a conserved tryptophan side chain at the membrane-distal end of a cadherin molecule from one cell, which inserts into a hydrophobic pocket at the membrane-distal end of a cadherin molecule from the opposing cell.

PubMed: 11964443
DOI: 10.1126/science.1071559

実験手法

X-RAY DIFFRACTION (3.08 Å)