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7Y54

Crystal structure of sDscam Ig1 domain, isoform alpha1

Summary for 7Y54
Entry DOI10.2210/pdb7y54/pdb
DescriptorDown Syndrome Cell Adhesion Molecules (2 entities in total)
Functional Keywordscell surface receptor, cell adhesion
Biological sourceChelicerata
Total number of polymer chains1
Total formula weight11023.51
Authors
Chen, Q.,Yu, Y.,Cheng, J. (deposition date: 2022-06-16, release date: 2023-05-24, Last modification date: 2024-10-23)
Primary citationCheng, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.787 Å)
Structure validation

240971

数据于2025-08-27公开中

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