Sandbox GGC5: Difference between revisions
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=='''Titin'''== | =='''Titin'''== | ||
<StructureSection load='1TIT' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1TIT' size='340' side='right' caption='Caption for this structure' scene=''> | ||
Titin,one of the largest human protein, in its longest isoform, has a molecular weight exceeding 3 MDa and is over 1.5 μm in length. Titin typically contains immunoglobulin (Ig) domains which are typically 110 amino acids in length, contain an internal disulfide bond and two layers of β-pleated sheets.<ref>PMID:31856237</ref> On the cellular level, titin is typically located within the nucleus of the cell; however, it can also be located within the cytoplasm. <ref>DOI 10.1002/ijch.201300024</ref> | Titin, one of the largest human protein, in its longest isoform, has a molecular weight exceeding 3 MDa and is over 1.5 μm in length. Titin typically contains immunoglobulin (Ig) domains which are typically 110 amino acids in length, contain an internal disulfide bond and two layers of β-pleated sheets.<ref>PMID:31856237</ref> On the cellular level, titin is typically located within the nucleus of the cell; however, it can also be located within the cytoplasm. <ref>DOI 10.1002/ijch.201300024</ref> | ||
== '''Function''' == | == '''Function''' == | ||
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== '''Relevance''' == | == '''Relevance''' == | ||
Titin is a flexible filament containing a beaded substructure indicating the presence of multiple domains within the molecule. These multiple domains include: the immunoglobulin domain, the Fibronectin type-II domain, the PEVK (proline-glutamate-valine-lysine-enriched unique sequence region, the unique sequences and the kinase domain. <ref name="figure" /> | |||
[[Image:Titin.JPG]] | [[Image:Titin.JPG]] | ||
'''This figure illustrates the ability of titin to coil and extend during muscle contraction and extension.'''<ref name="figure">PMID:10895161</ref> | '''This figure illustrates the ability of titin to coil and extend during muscle contraction and extension.'''<ref name="figure">PMID:10895161</ref> | ||
When the muscle contracts, the sarcomere length decreases resulting in the coiling of the I-band part of the titin. As the muscle extends, the sarcomere length increases resulting in the extension of titin. In the event of over-extension of the muscles there is unravelling of the titin peptide, starting in the least mechanically stable PEVK domain. <ref name="figure" /> | |||
== '''Structural highlights''' == | == '''Structural highlights''' == | ||
