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6CGU

mouse cadherin-6 EC1-2 adhesive fragment

Summary for 6CGU
Entry DOI10.2210/pdb6cgu/pdb
Related6CG6 6CG7 6CGB 6CGU
DescriptorCadherin-6, CALCIUM ION (3 entities in total)
Functional Keywordscadherin ec domain dimer extracellular, cell adhesion
Biological sourceMus musculus (Mouse)
Total number of polymer chains4
Total formula weight93123.58
Authors
Brasch, J.,Harrison, O.J.,Shapiro, L. (deposition date: 2018-02-20, release date: 2018-05-09, Last modification date: 2023-10-04)
Primary citationBrasch, J.,Katsamba, P.S.,Harrison, O.J.,Ahlsen, G.,Troyanovsky, R.B.,Indra, I.,Kaczynska, A.,Kaeser, B.,Troyanovsky, S.,Honig, B.,Shapiro, L.
Homophilic and Heterophilic Interactions of Type II Cadherins Identify Specificity Groups Underlying Cell-Adhesive Behavior.
Cell Rep, 23:1840-1852, 2018
Cited by
PubMed Abstract: Type II cadherins are cell-cell adhesion proteins critical for tissue patterning and neuronal targeting but whose molecular binding code remains poorly understood. Here, we delineate binding preferences for type II cadherin cell-adhesive regions, revealing extensive heterophilic interactions between specific pairs, in addition to homophilic interactions. Three distinct specificity groups emerge from our analysis with members that share highly similar heterophilic binding patterns and favor binding to one another. Structures of adhesive fragments from each specificity group confirm near-identical dimer topology conserved throughout the family, allowing interface residues whose conservation corresponds to specificity preferences to be identified. We show that targeted mutation of these residues converts binding preferences between specificity groups in biophysical and co-culture assays. Our results provide a detailed understanding of the type II cadherin interaction map and a basis for defining their role in tissue patterning and for the emerging importance of their heterophilic interactions in neural connectivity.
PubMed: 29742438
DOI: 10.1016/j.celrep.2018.04.012
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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數據於2024-11-06公開中

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