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==Crystal structure of chicken T-cadherin EC1 EC2==
==Crystal structure of chicken T-cadherin EC1 EC2==
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== Introduction == <StructureSection load='3k5s' size='240' side='none'caption='[[3k5s]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Introduction ==
The Cadherins are membrane proteins that mediate cell–cell adhesion and are essential for the development and structural integrity of tissues​ at the cellular level. Classical cadherins make up much of the cadherin family, such as E-, N-, and P-cadherins, which 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 their strand swapping are the standard for many organisms because of their adhesion strength and stability due to their membrane integration and low extracellular motility.
The Cadherins are membrane proteins that mediate cell–cell adhesion and are essential for the development and structural integrity of tissues​ at the cellular level. Classical cadherins make up much of the cadherin family, such as E-, N-, and P-cadherins, which 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 their strand swapping are the standard for many organisms because of their adhesion strength and stability due to their membrane integration and low extracellular motility.
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<StructureSection load='3k5s' size='240' side='none'caption='[[3k5s]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
T-Cadherins, truncated cadherins, are a sect of nonclassical cadherin, unique molecules that distinguish themselves from the above with different membrane anchorage techniques and functions, while retaining similar motifs and structures. Strand swapping and membrane integration, the two aspects of cadherins that allow them to provide structure and communication, are absent in T-cadherins as they lack the Trp-containing residues for strand swapping and the hydrophobic a-helix for membrane integration.
T-Cadherins, truncated cadherins, are a sect of nonclassical cadherin, unique molecules that distinguish themselves from the above with different membrane anchorage techniques and functions, while retaining similar motifs and structures. Strand swapping and membrane integration, the two aspects of cadherins that allow them to provide structure and communication, are absent in T-cadherins as they lack the Trp-containing residues for strand swapping and the hydrophobic a-helix for membrane integration.
== Function ==
== Function ==

Revision as of 16:17, 30 April 2025

Crystal structure of chicken T-cadherin EC1 EC2

Introduction

The Cadherins are membrane proteins that mediate cell–cell adhesion and are essential for the development and structural integrity of tissues​ at the cellular level. Classical cadherins make up much of the cadherin family, such as E-, N-, and P-cadherins, which 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 their strand swapping are the standard for many organisms because of their adhesion strength and stability due to their membrane integration and low extracellular motility.

PDB ID 3k5s

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References

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Jordan RG Elliott

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