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Function

Epithelial-cadherin (1-213), or E-cadherin is a calcium-dependent cell adhesion protein. E-cadherin regulates cell-to-cell interactions, adhesion of bacteria to mammalian cells, and cell mobility. E-cadherin also plays a crucial role in the normal blastula formation in several animal cells.

Relevance

E-cadherin is a tumor suppressor gene. Degradation or loss of function of the gene is associated with increased proliferation and metastasis of tumors. Since E-cadherin is related to the adhesion strength within epithelial tissue, a decrease in the ability or quantity of E-cadherin allows for increased cell mobility. This may allow cancerous cells to proliferate more rapidly and invade nearby tissues at a higher rate. Mutations in the E-cadherin protein are linked to a series of cancers, including gastric, thyroid, colorectal, breast, and ovarian cancers.

Structural highlights

E-cadherin 1 is 213 amino acids long. E-cadherin is composed of five cadherin extensions, a transmembrane region, and a cytoplasmic tail. E-cadherin cell-to-cell junctions are often located close to actin-filaments within the cytoskeleton of a cell.

The backbone of human E-cadherin is made up of two major parts, the beta-sheets and the helix region. Beta- sheets are a secondary structure in the E-cadherin molecule. Binding between beta-sheet regions of different E-cadherin molecules helps facilitate intermolecular adhesion. Beta-sheets allow binding between E-cadherin molecules in both monomer and dimer states (i.e. can bind as single molecules or to a chain of already bound molecules.)

References

https://www.ebi.ac.uk/pdbe/entry/pdb/2o72/biology http://www.uniprot.org/uniprot/P12830 https://en.wikipedia.org/wiki/CDH1_(gene)