Sandbox Reserved 773: Difference between revisions
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Each monomer is divided into 3 structural domains: N-terminal (2-71), large domain (71-371), and small domain (372-477) (green link/figure 5) <ref name=jbc/>. A monomer is also composed of 49% helical structure and 13% beta sheet <ref name=4e10/>. One specifically long α-helix which span from Valine-359 to Arginine-393 connects the large and small domains together (Figure 2). Through hydrophobic effect, the N-terminal regions of the two monomers interact with each other extensively. At the same time, the large domains interact extensively due to electrostatic interactions. Thus, the N-terminal regions and large domains form the dimer interfaces of HDC <ref name=jbc/>. | Each monomer is divided into 3 structural domains: N-terminal (2-71), large domain (71-371), and small domain (372-477) (green link/figure 5) <ref name=jbc/>. A monomer is also composed of 49% helical structure and 13% beta sheet <ref name=4e10/>. One specifically long α-helix which span from Valine-359 to Arginine-393 connects the large and small domains together (Figure 2). Through hydrophobic effect, the N-terminal regions of the two monomers interact with each other extensively. At the same time, the large domains interact extensively due to electrostatic interactions. Thus, the N-terminal regions and large domains form the dimer interfaces of HDC <ref name=jbc/>. | ||
<Structure load='4e1o' size='500' frame='true' align='right' caption=' | <Structure load='4e1o' size='500' frame='true' align='right' caption='Asymmetric unit of Histidine Decarboxylase complex with 6 PLP-HME substrate-analogs (atoms shown in orange, grey, and blue) bound to each of the active sites.' scene='Insert optional scene name here' /> | ||
== Cofactor and Substrate Binding Pocket == | == Cofactor and Substrate Binding Pocket == | ||
