Sandbox Reserved 1709: Difference between revisions

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=== Cap Domain ===

A key part of VKOR is the function of the <scene name='90/904314/ cap_domain/3'>Cap Domain</scene>, which is located right above the helices of VKOR towards the intracellular part of the membrane. The cap ~~is in~~ a helical shape and is located in close proximity to the Anchor and beta hairpin to maintain in the proper orientation. The cap domain assists with activating Vitamin K as it induces the structural change of VKOR from the open conformation to the closed conformation ~~when the~~ substrate ~~binds~~. ~~This~~ 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 ~~S43~~ and ~~S51~~, and polar interactions from D44.

A key part of VKOR is the function of the <scene name='90/904314/ cap_domain/3'>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. Catalytic cysteines help facilitate this transition from the open conformation to the closed conformation in order to assist with activation of Vitamin K.

=== Anchor ===

Sandbox Reserved 1709: Difference between revisions

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@@ Line 17: / Line 17: @@
 === Cap Domain ===
-A key part of VKOR is the function of the <scene name='90/904314/ cap_domain/3'>Cap Domain</scene>, which is located right above the helices of VKOR towards the intracellular part of the membrane. The cap is in a helical shape and is located in close proximity to the Anchor and beta hairpin to maintain in the proper orientation. The cap domain assists with activating Vitamin K as it induces the structural change of VKOR from the open conformation to the closed conformation when the substrate binds. This 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 S43 and S51, and polar interactions from D44.
+A key part of VKOR is the function of the <scene name='90/904314/ cap_domain/3'>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. Catalytic cysteines help facilitate this transition from the open conformation to the closed conformation in order to assist with activation of Vitamin K.
 === Anchor ===