Structural Basis of Adhesive Binding by Desmocollins and Desmogleins
Structural basis of adhesive binding by desmocollins and desmogleins Oliver J. Harrisona,b,1, Julia Braschc,1, Gorka Lassoa,d, Phinikoula S. Katsambaa,b, Goran Ahlsena,b, Barry Honiga,b,c,d,e,f,2, and Lawrence Shapiroa,c,f,2 aDepartment of Systems Biology, Columbia University, New York, NY 10032; bHoward Hughes Medical Institute, Columbia University, New York, NY 10032; cDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032; dCenter for Computational Biology and Bioinformatics, Columbia University, New York, NY 10032; eDepartment of Medicine, Columbia University, New York, NY 10032; and fZuckerman Mind Brain Behavior Institute, Columbia University, New York, NY 10032 Contributed by Barry Honig, April 23, 2016 (sent for review January 21, 2016; reviewed by Steven C. Almo and Dimitar B. Nikolov) Desmosomes are intercellular adhesive junctions that impart dense midline, consistent with a strand-swap mode of interaction first strength to vertebrate tissues. Their dense, ordered intercellular characterized for classical cadherins (19, 20). Nevertheless, the attachments are formed by desmogleins (Dsgs) and desmocollins identity of Dscs and Dsgs in these tomographic reconstructions could (Dscs), but the nature of trans-cellular interactions between these not be determined, and atomic-resolution structures of desmosomal specialized cadherins is unclear. Here, using solution biophysics and cadherins have not been available, with the exception of an NMR coated-bead aggregation experiments, we demonstrate family-wise structure of a monomeric EC1 fragment of mouse Dsg2 with an heterophilic specificity: All Dsgs form adhesive dimers with all Dscs, artificially extended N terminus (PDB ID code 2YQG). In addition, a with affinities characteristic of each Dsg:Dsc pair.
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