6ULM
Crystal structure of human cadherin 17 EC1-2
Summary for 6ULM
| Entry DOI | 10.2210/pdb6ulm/pdb |
| Descriptor | Cadherin-17, CALCIUM ION (3 entities in total) |
| Functional Keywords | cdh17, intestinal epithelia, cancer, calcium-binding, cell adhesion |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 51621.88 |
| Authors | Gray, M.E.,Sotomayor, M. (deposition date: 2019-10-08, release date: 2021-03-17, Last modification date: 2023-10-11) |
| Primary citation | Gray, M.E.,Sotomayor, M. Crystal structure of the nonclassical cadherin-17 N-terminus and implications for its adhesive binding mechanism. Acta Crystallogr.,Sect.F, 77:85-94, 2021 Cited by PubMed Abstract: The cadherin superfamily of calcium-dependent cell-adhesion proteins has over 100 members in the human genome. All members of the superfamily feature at least a pair of extracellular cadherin (EC) repeats with calcium-binding sites in the EC linker region. The EC repeats across family members form distinct complexes that mediate cellular adhesion. For instance, classical cadherins (five EC repeats) strand-swap their N-termini and exchange tryptophan residues in EC1, while the clustered protocadherins (six EC repeats) use an extended antiparallel `forearm handshake' involving repeats EC1-EC4. The 7D-cadherins, cadherin-16 (CDH16) and cadherin-17 (CDH17), are the most similar to classical cadherins and have seven EC repeats, two of which are likely to have arisen from gene duplication of EC1-2 from a classical ancestor. However, CDH16 and CDH17 lack the EC1 tryptophan residue used by classical cadherins to mediate adhesion. The structure of human CDH17 EC1-2 presented here reveals features that are not seen in classical cadherins and that are incompatible with the EC1 strand-swap mechanism for adhesion. Analyses of crystal contacts, predicted glycosylation and disease-related mutations are presented along with sequence alignments suggesting that the novel features in the CDH17 EC1-2 structure are well conserved. These results hint at distinct adhesive properties for 7D-cadherins. PubMed: 33682793DOI: 10.1107/S2053230X21002247 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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