User:Jordan RG Elliott/Sandbox 1

Function

The Cadherins are calcium-dependent proteins that mediate cell–cell adhesion and are essential for the development and structural integrity of tissues​ at the cellular level. Classical cadherins that make up much of the cadherin family, such as E-, N-, and P-cadherins, typically facilitate homophilic adhesion through a mechanism known as “strand swapping,” in which the N-terminal β-strands of cadherin molecules from opposing cells are exchanged. (Gumbiner, B. Regulation of cadherin-mediated adhesion in morphogenesis. Nat Rev Mol Cell Biol 6, 622–634 (2005). https://doi.org/10.1038/nrm1699). Classical cadherins and strand swapping are the standard for many organisms because of their adhesion strength and stability due to their membrane integration and low extra cellular motility.

T-Cadherins, or truncated cadherins, are a subset of nonclassical cadherin, unique molecules that distinguishes themselves from the above with different membrane anchorage techniques and functions, while retaining similar motifs and overall structures. The 3K5S T-cadherin is attached peripherally to the cell surface, via a GPI anchor, having no inner membrane or cytoplasmic domain,​ shorteing the total weight, hence the name truncated. (Ciatto, C., Bahna, F., Zampieri, N. et al. T-cadherin structures reveal a novel adhesive binding mechanism. Nat Struct Mol Biol 17, 339–347 (2010). https://doi.org/10.1038/nsmb.1781) This binding method and reduced size is beneficial for 3K5S while acting as a neurite development and signaling aid in chick growth. The increased mobility and lack of rigid structure can allow for a more fluid and less tense growth environment for development.

Disease

Relevance

Structural highlights

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