Sandbox Reserved 1709: Difference between revisions

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=== Cap Domain ===

[[Image:VKOR_in_cell_membrane.png|500 px|right|thumb|Figure 2. Orientation and interactions of the VKOR components cap domain, anchor domain, and helical tunnel within the cell membrane.]]

A key part of VKOR is the function of the <scene name='90/904314/Cap_domain/6'>cap domain</scene>, which is located right above the helices of VKOR towards the intracellular part of the membrane. The cap has a helical shape and is located in close proximity to two other domains: the Anchor domain and beta hairpin. This combination of domains help to maintain the proper orientation in the membrane. The cap domain assists with activating Vitamin K as it induces the structural change of VKOR from the open conformation to the closed conformation upon substrate binding. Cap rearrangement and transition to the closed conformation initiates a domino effect through the [https://reader.elsevier.com/reader/sd/pii/S0021925820001386?token=9F8E1964241D20488CA55E035D35D9A5D650A7B3FDAD9A5579598A8DC00127539BE71CF1785B117102144AC1F41ABB6C&originRegion=us-east-1&originCreation=20220329001707/ catalytic mechanism]. The cap domain has critical interactions that stabilize the closed conformation including a <scene name='90/904314/Disulfide_bridge_stabilization/3'> disulfide bridge</scene> between C43 and C51, and polar interactions from D44. These interactions are broken up by reactive cysteines to induce different conformations and help facilitate this transition from the open conformation to the closed conformation during the activation of Vitamin K.

A key part of VKOR is the function of the <scene name='90/904314/Cap_domain/6'>cap domain</scene>, which is located right above the helices of VKOR towards the intracellular part of the membrane. The cap has a helical shape and is located in close proximity to two other domains: the Anchor domain and beta hairpin. This combination of domains help to maintain the proper orientation in the membrane. The cap domain assists with activating Vitamin K as it induces the structural change of VKOR from the open conformation to the closed conformation upon substrate binding. Cap rearrangement and transition to the closed conformation initiates a domino effect through the [https://reader.elsevier.com/reader/sd/pii/S0021925820001386?token=9F8E1964241D20488CA55E035D35D9A5D650A7B3FDAD9A5579598A8DC00127539BE71CF1785B117102144AC1F41ABB6C&originRegion=us-east-1&originCreation=20220329001707/ catalytic mechanism]. The cap domain has critical interactions that stabilize the closed conformation including a <scene name='90/904314/Disulfide_bridge_stabilization/5'>disulfide bridge</scene> between C43 and C51, and polar interactions from D44. These interactions are broken up by reactive cysteines to induce different conformations and help facilitate this transition from the open conformation to the closed conformation during the activation of Vitamin K.

=== Anchor ===

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@@ Line 18: / Line 18: @@
 === Cap Domain ===
 [[Image:VKOR_in_cell_membrane.png|500 px|right|thumb|Figure 2. Orientation and interactions of the VKOR components cap domain, anchor domain, and helical tunnel within the cell membrane.]]
-A key part of VKOR is the function of the <scene name='90/904314/Cap_domain/6'>cap domain</scene>, which is located right above the helices of VKOR towards the intracellular part of the membrane. The cap has a helical shape and is located in close proximity to two other domains: the Anchor domain and beta hairpin. This combination of domains help to maintain the proper orientation in the membrane. The cap domain assists with activating Vitamin K as it induces the structural change of VKOR from the open conformation to the closed conformation upon substrate binding. Cap rearrangement and transition to the closed conformation initiates a domino effect through the [https://reader.elsevier.com/reader/sd/pii/S0021925820001386?token=9F8E1964241D20488CA55E035D35D9A5D650A7B3FDAD9A5579598A8DC00127539BE71CF1785B117102144AC1F41ABB6C&originRegion=us-east-1&originCreation=20220329001707/ catalytic mechanism]. The cap domain has critical interactions that stabilize the closed conformation including a <scene name='90/904314/Disulfide_bridge_stabilization/3'> disulfide bridge</scene> between C43 and C51, and polar interactions from D44. These interactions are broken up by reactive cysteines to induce different conformations and help facilitate this transition from the open conformation to the closed conformation during the activation of Vitamin K.
+A key part of VKOR is the function of the <scene name='90/904314/Cap_domain/6'>cap domain</scene>, which is located right above the helices of VKOR towards the intracellular part of the membrane. The cap has a helical shape and is located in close proximity to two other domains: the Anchor domain and beta hairpin. This combination of domains help to maintain the proper orientation in the membrane. The cap domain assists with activating Vitamin K as it induces the structural change of VKOR from the open conformation to the closed conformation upon substrate binding. Cap rearrangement and transition to the closed conformation initiates a domino effect through the [https://reader.elsevier.com/reader/sd/pii/S0021925820001386?token=9F8E1964241D20488CA55E035D35D9A5D650A7B3FDAD9A5579598A8DC00127539BE71CF1785B117102144AC1F41ABB6C&originRegion=us-east-1&originCreation=20220329001707/ catalytic mechanism]. The cap domain has critical interactions that stabilize the closed conformation including a <scene name='90/904314/Disulfide_bridge_stabilization/5'>disulfide bridge</scene> between C43 and C51, and polar interactions from D44. These interactions are broken up by reactive cysteines to induce different conformations and help facilitate this transition from the open conformation to the closed conformation during the activation of Vitamin K.
 === Anchor ===