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5XWX

Crystal structure of the four N-terminal immunoglogulin domains of Sidekick-1 protein

5XWX の概要
エントリーDOI10.2210/pdb5xwx/pdb
分子名称Protein sidekick-1 (2 entities in total)
機能のキーワードcell-cell adhesion, cell adhesion
由来する生物種Mus musculus (Mouse)
タンパク質・核酸の鎖数2
化学式量合計100736.77
構造登録者
Tang, H.,Dong, Y.,He, Y. (登録日: 2017-06-30, 公開日: 2018-08-29, 最終更新日: 2024-11-13)
主引用文献Tang, H.,Chang, H.,Dong, Y.,Guo, L.,Shi, X.,Wu, Y.,Huang, Y.,He, Y.
Architecture of cell-cell adhesion mediated by sidekicks.
Proc. Natl. Acad. Sci. U.S.A., 115:9246-9251, 2018
Cited by
PubMed Abstract: Cell-cell adhesion is important for cell growth, tissue development, and neural network formation. Structures of cell adhesion molecules have been widely studied by crystallography, revealing the molecular details of adhesion interfaces. However, due to technical limitations, the overall structure and organization of adhesion molecules at cell adhesion interfaces has not been fully investigated. Here, we combine electron microscopy and other biophysical methods to characterize the structure of cell-cell adhesion mediated by the cell adhesion molecule Sidekick (Sidekick-1 and Sidekick-2) and obtain 3D views of the Sidekick-mediated adhesion interfaces as well as the organization of Sidekick molecules between cell membranes by electron tomography. The results suggest that the Ig-like domains and the fibronectin III (FnIII) domains of Sidekicks play different roles in cell adhesion. The Ig-like domains mediate the homophilic transinteractions bridging adjacent cells, while the FnIII domains interact with membranes, resulting in a tight adhesion interface between cells that may contribute to the specificity and plasticity of cell-cell contacts during cell growth and neural development.
PubMed: 30150416
DOI: 10.1073/pnas.1801810115
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.55 Å)
構造検証レポート
Validation report summary of 5xwx
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-13に公開中

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