Sandbox Reserved 1710: Difference between revisions

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In the <scene name='90/904315/Open_conformation/4'>open, active conformation</scene>, (REWRITE ABOUT RAS REGULATION)

This transition is initiated by movement of the transition metal-binding site. The Cys 1032, His 1558, and His 1576 Residues become separated and zinc is not able to bond. In the active form, one protomer has its GRD and Sec14-PH domains oriented oppositely from the inactive form. The GRD rotates -130° and the Sec14-PH domain rotates -90° (TOWARDS WHAT?) Due to this rotation, Cys 1032 is now located too far away, approximately 30 Å, from His 1558 and His 1576 which results in the loss of the metal-binding site and no formation of the <scene name='90/904315/Open_conformation_triade/4'>triad</scene>. The lack of the transition metal-binding site allows the GRD to orient itself to associate with <scene name='90/904315/Ras_open_conformation/3'>Ras</scene>. This association positions the <scene name='90/904315/Open_conformation_arginine_fin/2'>Arginine Finger</scene> (TO DO WHAT?). When Neurofibromin is in the open, active conformation, Arg 1276 is able to <scene name='90/904315/Ras_open_conformation_with_arg/2'>bind to Ras</scene> because there is no steric hindrance from the Neurofibromin core.

This transition is initiated by movement of the transition metal-binding site. The Cys 1032, His 1558, and His 1576 Residues become separated and zinc is not able to bond. In the active form, one protomer has its GRD and Sec14-PH domains oriented oppositely from the inactive form. The GRD rotates -130° and the Sec14-PH domain rotates -90° (TOWARDS WHAT?) Due to this rotation, Cys 1032 is now located too far away, approximately 30 Å, from His 1558 and His 1576 which results in the loss of the metal-binding site and no formation of the <scene name='90/904315/Open_conformation_triade/5'>triad</scene>. The lack of the transition metal-binding site allows the GRD to orient itself to associate with <scene name='90/904315/Ras_open_conformation/3'>Ras</scene>. This association positions the <scene name='90/904315/Open_conformation_arginine_fin/2'>Arginine Finger</scene> (TO DO WHAT?). When Neurofibromin is in the open, active conformation, Arg 1276 is able to <scene name='90/904315/Ras_open_conformation_with_arg/2'>bind to Ras</scene> because there is no steric hindrance from the Neurofibromin core.

[[Image:Domain Rotation.jpg|500 px|left|thumb|Figure 2: Rotation of the GRD and Sec14-PH domains from the closed conformation of neurofibromin to the open conformation of neurofibromin to allow Ras binding. The GRD rotates -130° and the Sec14-PH domain rotates -90°]]

Sandbox Reserved 1710: Difference between revisions

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@@ Line 26: / Line 26: @@
 In the <scene name='90/904315/Open_conformation/4'>open, active conformation</scene>,  (REWRITE ABOUT RAS REGULATION)
-This transition is initiated by movement of the transition metal-binding site. The Cys 1032, His 1558, and His 1576 Residues become separated and zinc is not able to bond. In the active form, one protomer has its GRD and Sec14-PH domains oriented oppositely from the inactive form. The GRD rotates -130° and the Sec14-PH domain rotates -90° (TOWARDS WHAT?) Due to this rotation, Cys 1032 is now located too far away, approximately 30 Å, from His 1558 and His 1576 which results in the loss of the metal-binding site and no formation of the <scene name='90/904315/Open_conformation_triade/4'>triad</scene>. The lack of the transition metal-binding site allows the GRD to orient itself to associate with <scene name='90/904315/Ras_open_conformation/3'>Ras</scene>. This association positions the <scene name='90/904315/Open_conformation_arginine_fin/2'>Arginine Finger</scene> (TO DO WHAT?). When Neurofibromin is in the open, active conformation, Arg 1276 is able to <scene name='90/904315/Ras_open_conformation_with_arg/2'>bind to Ras</scene> because there is no steric hindrance from the Neurofibromin core.
+This transition is initiated by movement of the transition metal-binding site. The Cys 1032, His 1558, and His 1576 Residues become separated and zinc is not able to bond. In the active form, one protomer has its GRD and Sec14-PH domains oriented oppositely from the inactive form. The GRD rotates -130° and the Sec14-PH domain rotates -90° (TOWARDS WHAT?) Due to this rotation, Cys 1032 is now located too far away, approximately 30 Å, from His 1558 and His 1576 which results in the loss of the metal-binding site and no formation of the <scene name='90/904315/Open_conformation_triade/5'>triad</scene>. The lack of the transition metal-binding site allows the GRD to orient itself to associate with <scene name='90/904315/Ras_open_conformation/3'>Ras</scene>. This association positions the <scene name='90/904315/Open_conformation_arginine_fin/2'>Arginine Finger</scene> (TO DO WHAT?). When Neurofibromin is in the open, active conformation, Arg 1276 is able to <scene name='90/904315/Ras_open_conformation_with_arg/2'>bind to Ras</scene> because there is no steric hindrance from the Neurofibromin core.
 [[Image:Domain Rotation.jpg|500 px|left|thumb|Figure 2: Rotation of the GRD and Sec14-PH domains from the closed conformation of neurofibromin to the open conformation of neurofibromin to allow Ras binding. The GRD rotates -130° and the Sec14-PH domain rotates -90°]]