Sandbox Reserved 773: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Wesley Yang (talk | contribs) |
Wesley Yang (talk | contribs) |
||
| Line 49: | Line 49: | ||
Each monomer is divided into 3 structural <scene name='56/564049/3domain/4'>domains</scene>. They are: the <scene name='56/564049/Nterminal/1'>N-terminal</scene> (~2-71), the <scene name='56/564049/Largedomain/3'>large domain</scene> (71-371), and the <scene name='56/564049/ | Each monomer is divided into 3 structural <scene name='56/564049/3domain/4'>domains</scene>. They are: the <scene name='56/564049/Nterminal/1'>N-terminal</scene> (~2-71), the <scene name='56/564049/Largedomain/3'>large domain</scene> (71-371), and the <scene name='56/564049/Sdomain/1'>small domain</scene> (372-477) (Figure 5) <ref name=jbc/>. A monomer is also composed of 49% <scene name='56/564049/Helix/2'>helices</scene> and 13% <scene name='56/564049/Sheet/1'>sheets</scene> (7 antiparallel and 4 parallel β-sheets)<ref name=4e10/>. One distinctively long α-<scene name='56/564049/Longhelix/1'>helix</scene> which span from Val-359 to Arg-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/>. | ||