5XX0

Crystal structure of the four N-terminal immunoglogulin domains of Sidekick-2 protein

5XX0 の概要

• エントリーDOI: 10.2210/pdb5xx0/pdb
• 分子名称: Protein sidekick-2 (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: 89634.27

構造登録者

Dong, Y.,Tang, H.,He, Y. (登録日: 2017-06-30, 公開日: 2018-08-29, 最終更新日: 2023-11-22)

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

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

実験手法

X-RAY DIFFRACTION (2.4 Å)