5XWX

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

Summary for 5XWX

• Entry DOI: 10.2210/pdb5xwx/pdb
• Descriptor: Protein sidekick-1 (2 entities in total)
• Functional Keywords: cell-cell adhesion, cell adhesion
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 2
• Total formula weight: 100736.77

Authors

Tang, H.,Dong, Y.,He, Y. (deposition date: 2017-06-30, release date: 2018-08-29, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.55 Å)