Sandbox Reserved 1726: Difference between revisions
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[[Image:glycinehelicesorange.png|300 px|right|thumb|Figure 2. Rare Glycine helices on Anaplastic Lymphoma Kinase]]Located between the THB-like domain and the TNF-like domain, the <scene name='90/904331/Polyg_region1/4'>Poly-Glycine Region</scene> has an important structural role. The GlyR domain also has a rare and unique structure of left-handed glycine helices with hexagonal hydrogen bonding shown in Figure 2. These 14 glycine helices are unique to ALK's function among other tyrosine kinases, as these types of structures on the binding domain are not present. These helices are rigid structures, providing a strong anchor for the ligand binding site while the other domains undergo drastic conformational rearrangements.<ref name="Reshetnyak" /> | [[Image:glycinehelicesorange.png|300 px|right|thumb|Figure 2. Rare Glycine helices on Anaplastic Lymphoma Kinase]]Located between the THB-like domain and the TNF-like domain, the <scene name='90/904331/Polyg_region1/4'>Poly-Glycine Region</scene> has an important structural role. The GlyR domain also has a rare and unique structure of left-handed glycine helices with hexagonal hydrogen bonding shown in Figure 2. These 14 glycine helices are unique to ALK's function among other tyrosine kinases, as these types of structures on the binding domain are not present. These helices are rigid structures, providing a strong anchor for the ligand binding site while the other domains undergo drastic conformational rearrangements.<ref name="Reshetnyak" /> | ||
==== Tumor-Necrosis Factor-like Domain ==== | ==== Tumor-Necrosis Factor-like Domain ==== | ||
The <scene name='90/ | The <scene name='90/904332/Tnf-like_domain/2'>Tumor Necrosis Factor-like Domain</scene> interacts with the THB-like domain to begin the conformational changes associated with ligand binding. It is located in approximately the midregion of the extracellular region, bridging the gap between the GlyR domain and the EGF-like domain. This domain also assists in mediating ligand binding with the EGF-like domain. In ligand-binding, as previously stated, this domain interacts heavily with the THB-like domain to undergo critical conformation changes necessary for dimerization and ligand recognition. <ref name="Reshetnyak" /> | ||
==== Epidermal Growth Factor-like Domain ==== | ==== Epidermal Growth Factor-like Domain ==== | ||
The <scene name='90/904331/Egf_like_domain/2'>Epidermal Growth Factor-like Domain</scene> is very malleable and repositioning of this domain is essential for activation of the protein. This domain is able to undergo conformational changes with the ligand bound and when in contact with the TNF-like domain. The interface between the EGF-like and TNF-like domains are primarily hydrophobic residues, which enable their flexibility with regards to one another. The main motifs that are apart of the EGF-like domain are major and minor β-hairpins, which are stabilized by 3 conserved disulfide bridges. <ref name="Reshetnyak" /> | The <scene name='90/904331/Egf_like_domain/2'>Epidermal Growth Factor-like Domain</scene> is very malleable and repositioning of this domain is essential for activation of the protein. This domain is able to undergo conformational changes with the ligand bound and when in contact with the TNF-like domain. The interface between the EGF-like and TNF-like domains are primarily hydrophobic residues, which enable their flexibility with regards to one another. The main motifs that are apart of the EGF-like domain are major and minor β-hairpins, which are stabilized by 3 conserved disulfide bridges. <ref name="Reshetnyak" /> | ||