2O72

Crystal Structure Analysis of human E-cadherin (1-213)

2O72 の概要

• エントリーDOI: 10.2210/pdb2o72/pdb
• 分子名称: Epithelial-cadherin, CALCIUM ION (3 entities in total)
• 機能のキーワード: ig-like domains, calcium-binding protein, cell adhesion, metal binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell junction : P12830
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23335.05

構造登録者

Parisini, E.,Wang, J.-H. (登録日: 2006-12-09, 公開日: 2007-10-09, 最終更新日: 2023-08-30)

主引用文献

Parisini, E.,Higgins, J.M.G.,Liu, J.-H.,Brenner, M.B.,Wang, J.-H.
The Crystal Structure of Human E-cadherin Domains 1 and 2, and Comparison with other Cadherins in the Context of Adhesion Mechanism
J.Mol.Biol., 373:401-411, 2007

PubMed Abstract: Cell adhesion mediated by type I cadherins involves homophilic "trans" interactions that are thought to be brought about by a strand exchange mechanism involving the N-terminal extracellular domain. Here, we present the high-resolution crystal structure of the N-terminal two domains of human E-cadherin. Comparison of this structure with other type I cadherin structures reveals features that are likely to be critical to facilitate dimerization by strand exchange as well as dimer flexibility. We integrate this structural knowledge to provide a model for type I cadherin adhesive interactions. Intra-molecular docking of the conserved N-terminal "adhesion arm" into the acceptor pocket in monomeric E-cadherin appears largely identical to inter-molecular docking of the adhesion arm in adhesive trans dimers. A strained conformation of the adhesion arm in the monomer, however, may create an equilibrium between "open" and "closed" forms that primes the cadherin for formation of adhesive interactions, which are then stabilized by additional dimer-specific contacts. By contrast, in type II cadherins, strain in the adhesion arm appears absent and a much larger surface area is involved in trans adhesion, which may compensate the activation energy required to peel off the intra-molecularly docked arm. It seems that evolution has selected slightly different adhesion mechanisms for type I and type II cadherins.

PubMed: 17850815
DOI: 10.1016/j.jmb.2007.08.011

実験手法

X-RAY DIFFRACTION (2 Å)