Sandbox Reserved 1713: Difference between revisions
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== Structure & Function == | == Structure & Function == | ||
===Domains=== | |||
The extracellular portion of ALK has an inactive state, which is its monomerized form, and an active dimerized state with its ligands bound. The monomer is shown to the right in Figure 1, which has many different domains. The growth factor-like domain (EGF) connects the extracellular domains to the transmembrane domain (cyan). The tumor necrosis factor-like domain (TNFL) has a beta-sandwich structure that provides important residues that act as the binding surface for the ligand(orange). The glycine-rich domain (GlyR) contains 14 rare polyglycine helices that are hydrogen-bound to each other (green). The <scene name='90/904318/Glycinerichdomain/1'>hexagonal orientation</scene> of these rare helices create a very rigid structure that is important for ALK function. The polyglycine extension loop (PXL) connects two of these polyglycine helices. | The extracellular portion of ALK has an inactive state, which is its monomerized form, and an active dimerized state with its ligands bound. The monomer is shown to the right in Figure 1, which has many different domains. The growth factor-like domain (EGF) connects the extracellular domains to the transmembrane domain (cyan). The tumor necrosis factor-like domain (TNFL) has a beta-sandwich structure that provides important residues that act as the binding surface for the ligand(orange). The glycine-rich domain (GlyR) contains 14 rare polyglycine helices that are hydrogen-bound to each other (green). The <scene name='90/904318/Glycinerichdomain/1'>hexagonal orientation</scene> of these rare helices create a very rigid structure that is important for ALK function. The polyglycine extension loop (PXL) connects two of these polyglycine helices. | ||
The domains that aren't shown in Figure 1 but are shown in the domain map (Figure 2) that also make up the monomer are the heparin binding domains (HBDs), which are at the N-terminal end of the monomer. Heparin has been found to be a possible activating ligand of ALK. The transmembrane domain (TMH) are the residues of ALK that are located within the membrane. The kinase domain is the intracellular portion of ALK that contains the Tyr residues which are auto-phosphorylated when ALK is activated, initiating a signaling cascade. | |||
[[Image:Prote_ALK_Monomer_White.png|400 px|right|thumb|Figure 1]] | [[Image:Prote_ALK_Monomer_White.png|400 px|right|thumb|Figure 1]] | ||
[[Image:Proteo_ALK-ALKAL_Monomer_White.png|400 px|right|thumb|Figure 2]] | [[Image:Proteo_ALK-ALKAL_Monomer_White.png|400 px|right|thumb|Figure 2]] | ||