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(New page: {{Sandbox_Reserved_HLSC322}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> ==Your Heading Here (maybe something like 'Structure')== <StructureSection load='1stp' size='340' side='right' capti...) |
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{{Sandbox_Reserved_HLSC322}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_Reserved_HLSC322}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
| - | == | + | ==Human E-cadherin Protein== |
| - | <StructureSection load=' | + | <StructureSection load='2o72' size='340' side='right' caption='Caption for this structure' scene=''> |
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== Function == | == 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 == | == Relevance == | ||
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| + | 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 == | == 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. | |
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| + | <scene name='77/777712/Backbone_of_molecule/1'>Back bone of E-cadherin</scene> | ||
| + | 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.) <scene name='77/777712/Beta-sheets/1'>Beta sheets</scene> | ||
| - | </ | + | The helix region of the E-cadherin molecule prevents the abnormal regulation of the junction complex, thus ensuring complete and correct translation of the spliced mRNA into protein. <scene name='77/777712/Helix_region/1'>Helix Region</scene> |
== References == | == References == | ||
<references/> | <references/> | ||
| + | https://www.ebi.ac.uk/pdbe/entry/pdb/2o72/biology | ||
| + | http://www.uniprot.org/uniprot/P12830 | ||
| + | https://en.wikipedia.org/wiki/CDH1_(gene) | ||
Current revision
| This Sandbox is Reserved from January through July 31, 2018 for use in the course HLSC322: Principles of Genetics and Genomics taught by Genevieve Houston-Ludlam at the University of Maryland, College Park, USA. This reservation includes Sandbox Reserved 1311 through Sandbox Reserved 1430. |
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Human E-cadherin Protein
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