User:Jordan RG Elliott/Sandbox 1
From Proteopedia
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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 == |
The 3K5S T-cadherin is attached peripherally to the cell surface, via a GPI anchor, having no inner membrane or cytoplasmic domain, shortening the total weight and length of a single unit, hence the name truncated. (Ranscht B, Dours-Zimmermann MT. T-cadherin, a novel cadherin cell adhesion molecule in the nervous system, lacks the conserved cytoplasmic region. Neuron. 1991 Sep;7(3):391-402. doi: 10.1016/0896-6273(91)90291-7. PMID: 1654948.) This binding method and reduced size benefit 3K5S in its role of aiding neurite development and signaling in chick growth. The soft structure and shorter signalling reach allows for a more fluid and less tense growth environment for neural development. The concentration of 3K5S is slowly diminished as other cadherins, because more necessary for adult synaptic maintenance. (https://www.sciencedirect.com/science/article/pii/S0006899308002813#:~:text=Three%20types%20of%20full%2Dlength%20cDNAs%20encoding%20chicken,high%20similarity%20to%20rat%20and%20human%20Cdh8.) | The 3K5S T-cadherin is attached peripherally to the cell surface, via a GPI anchor, having no inner membrane or cytoplasmic domain, shortening the total weight and length of a single unit, hence the name truncated. (Ranscht B, Dours-Zimmermann MT. T-cadherin, a novel cadherin cell adhesion molecule in the nervous system, lacks the conserved cytoplasmic region. Neuron. 1991 Sep;7(3):391-402. doi: 10.1016/0896-6273(91)90291-7. PMID: 1654948.) This binding method and reduced size benefit 3K5S in its role of aiding neurite development and signaling in chick growth. The soft structure and shorter signalling reach allows for a more fluid and less tense growth environment for neural development. The concentration of 3K5S is slowly diminished as other cadherins, because more necessary for adult synaptic maintenance. (https://www.sciencedirect.com/science/article/pii/S0006899308002813#:~:text=Three%20types%20of%20full%2Dlength%20cDNAs%20encoding%20chicken,high%20similarity%20to%20rat%20and%20human%20Cdh8.) | ||
== Structural Highlights == | == Structural Highlights == | ||
| - | + | <StructureSection load='3k5s' size='240' side='none'caption='[[3k5s]], [[Resolution|resolution]] 2.90Å' scene=''> | |
<table><tr><td colspan='2'> | <table><tr><td colspan='2'> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
Revision as of 16:18, 30 April 2025
Contents |
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.
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
The 3K5S T-cadherin is attached peripherally to the cell surface, via a GPI anchor, having no inner membrane or cytoplasmic domain, shortening the total weight and length of a single unit, hence the name truncated. (Ranscht B, Dours-Zimmermann MT. T-cadherin, a novel cadherin cell adhesion molecule in the nervous system, lacks the conserved cytoplasmic region. Neuron. 1991 Sep;7(3):391-402. doi: 10.1016/0896-6273(91)90291-7. PMID: 1654948.) This binding method and reduced size benefit 3K5S in its role of aiding neurite development and signaling in chick growth. The soft structure and shorter signalling reach allows for a more fluid and less tense growth environment for neural development. The concentration of 3K5S is slowly diminished as other cadherins, because more necessary for adult synaptic maintenance. (https://www.sciencedirect.com/science/article/pii/S0006899308002813#:~:text=Three%20types%20of%20full%2Dlength%20cDNAs%20encoding%20chicken,high%20similarity%20to%20rat%20and%20human%20Cdh8.)
Structural Highlights
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