Sandbox Reserved 1709: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 12: | Line 12: | ||
===Structural Overview=== | ===Structural Overview=== | ||
VKOR has many key components of its structure that allow it to maintain proper functionality and catalytic abilities. The VKOR active site allows for specific substrate binding via many highly conserved residues that can recognize the target substrates. It works in conjunction with the cap domain, which is a helical component of the VKOR that facilitates the conformation from the open to closed conformation of the enzyme once the substrate binds. Interactions between this domain, the active site, and the bound protein are critical to achieve full activation of Vitamin K. Another important part of the structure is the anchor, which simply serves as a way to hold VKOR within the proper orientation in the cell membrane such that all enzymatic components are in correct proximity for substrate binding and catalysis. | VKOR has many key components of its structure that allow it to maintain proper functionality and catalytic abilities. The VKOR active site allows for specific substrate binding via many highly conserved residues that can recognize the target substrates. It works in conjunction with the cap domain, which is a helical component of the VKOR that facilitates the conformation from the open to closed conformation of the enzyme once the substrate binds. Interactions between this domain, the active site, and the bound protein are critical to achieve full activation of Vitamin K. Another important part of the structure is the anchor, which simply serves as a way to hold VKOR within the proper orientation in the cell membrane such that all enzymatic components are in correct proximity for substrate binding and catalysis. | ||
=== Active Site === | === Active Site === | ||
Within the four transmembrane helices lies the <scene name='90/906893/Active_site/4'> | Within the four transmembrane helices lies the <scene name='90/906893/Active_site/4'>binding pocket</scene>. The active site is comprised of a hydrophobic pocket containing two hydrophilic residues, N80 and Y139, that interact with substrates and ligands alike. The hydrophobic pocket provides specificity to the region while the hydrophilic residues hydrogen bond to the substrate, providing recognition and increasing specificity. The C132-C135 disulfide bridge above the binding pocket provides stabilization when a substrate is bound. This bridge provides increased stability for the binding site as it interacts with and binds substrates or inhibitors. Upon binding, VKOR will transition into the <scene name='90/906893/Closed_conformation/4'>closed conformation</scene> allowing the catalytic mechanism to commence. | ||
=== Cap Domain === | === Cap Domain === | ||
[[Image:VKOR_in_cell_membrane.png|400 px|right|thumb|Figure 2. Orientation and interactions of cap domain, anchor domain, and helical tunnel within the cell membrane.]] | [[Image:VKOR_in_cell_membrane.png|400 px|right|thumb|Figure 2. Orientation and interactions of cap domain, anchor domain, and helical tunnel within the cell membrane.]] | ||
