5ERP
Crystal structure of human Desmocollin-2 ectodomain fragment EC2-5
Summary for 5ERP
| Entry DOI | 10.2210/pdb5erp/pdb |
| Related | 5EQX 5ERD |
| Descriptor | Desmocollin-2, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose, ... (8 entities in total) |
| Functional Keywords | extracellular cadherin domain, cell adhesion, cell surface, desmosome |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 106359.01 |
| Authors | Harrison, O.J.,Brasch, J.,Shapiro, L. (deposition date: 2015-11-14, release date: 2016-06-15, Last modification date: 2023-09-27) |
| Primary citation | Harrison, O.J.,Brasch, J.,Lasso, G.,Katsamba, P.S.,Ahlsen, G.,Honig, B.,Shapiro, L. Structural basis of adhesive binding by desmocollins and desmogleins. Proc.Natl.Acad.Sci.USA, 113:7160-7165, 2016 Cited by PubMed Abstract: Desmosomes are intercellular adhesive junctions that impart strength to vertebrate tissues. Their dense, ordered intercellular attachments are formed by desmogleins (Dsgs) and desmocollins (Dscs), but the nature of trans-cellular interactions between these specialized cadherins is unclear. Here, using solution biophysics and coated-bead aggregation experiments, we demonstrate family-wise heterophilic specificity: All Dsgs form adhesive dimers with all Dscs, with affinities characteristic of each Dsg:Dsc pair. Crystal structures of ectodomains from Dsg2 and Dsg3 and from Dsc1 and Dsc2 show binding through a strand-swap mechanism similar to that of homophilic classical cadherins. However, conserved charged amino acids inhibit Dsg:Dsg and Dsc:Dsc interactions by same-charge repulsion and promote heterophilic Dsg:Dsc interactions through opposite-charge attraction. These findings show that Dsg:Dsc heterodimers represent the fundamental adhesive unit of desmosomes and provide a structural framework for understanding desmosome assembly. PubMed: 27298358DOI: 10.1073/pnas.1606272113 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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