7Y9A

Crystal structure of sDscam Ig1-2 domains, isoform beta2v6

Summary for 7Y9A

• Entry DOI: 10.2210/pdb7y9a/pdb
• Descriptor: Down Syndrome Cell Adhesion Molecules, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-3)][beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: cell surface receptor, cell adhesion
• Biological source: Chelicerata
• Total number of polymer chains: 1
• Total formula weight: 23088.71

Authors

Chen, Q.,Yu, Y.,Cheng, J. (deposition date: 2022-06-24, release date: 2023-05-24, Last modification date: 2024-10-09)

Primary citation

Cheng, J.,Yu, Y.,Wang, X.,Zheng, X.,Liu, T.,Hu, D.,Jin, Y.,Lai, Y.,Fu, T.M.,Chen, Q.
Structural basis for the self-recognition of sDSCAM in Chelicerata.
Nat Commun, 14:2522-2522, 2023

PubMed Abstract: To create a functional neural circuit, neurons develop a molecular identity to discriminate self from non-self. The invertebrate Dscam family and vertebrate Pcdh family are implicated in determining synaptic specificity. Recently identified in Chelicerata, a shortened Dscam (sDscam) has been shown to resemble the isoform-generating characters of both Dscam and Pcdh and represent an evolutionary transition. Here we presented the molecular details of sDscam self-recognition via both trans and cis interactions using X-ray crystallographic data and functional assays. Based on our results, we proposed a molecular zipper model for the assemblies of sDscam to mediate cell-cell recognition. In this model, sDscam utilized FNIII domain to form side-by-side interactions with neighboring molecules in the same cell while established hand-in-hand interactions via Ig1 domain with molecules from another cell around. Together, our study provided a framework for understanding the assembly, recognition, and evolution of sDscam.

PubMed: 37130844
DOI: 10.1038/s41467-023-38205-1

Experimental method

X-RAY DIFFRACTION (2.51 Å)