Sandbox Reserved 1710: Difference between revisions

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=== Closed Conformation ===

The first conformation of Neurofibromin is known as the <scene name='90/904315/Closed/2'>Closed Conformation</scene>, which is representative of an inactive Neurofibromin protein. In the closed conformation, both sets of the GRD and Sec14-PH domains are rotated in a way that they are inaccessible and inactive due to a <scene name='90/904315/Catalytic_triade/2'>triade</scene> consisting of residues Cysteine 1032, Histidine 1558, and Histidine 1576 that form a transition metal-binding site with zinc. The close proximity of the C1032, H1558, and H1576 residues that form the <scene name='90/904316/Closed_triade/1'>triade in ~~the~~ closed conformation</scene> keep the GRD domain packed tightly on top of the Neurofibromin core. This tight compaction leads to steric inhibition when Neurofibromin tries to perform its function and associate with Ras. The association between Ras and Neurofibromin is supposed to occur via an <scene name='90/904316/Arg_finger/2'>Arginine finger</scene> located at Residue 1276. However, the steric hindrance from the Neurofibromin core in the closed conformation inhibits this association. Therefore, when Neurofibromin is in the closed conformation, there is no association with Ras and cell growth and proliferation is able to occur.

The first conformation of Neurofibromin is known as the <scene name='90/904315/Closed/2'>Closed Conformation</scene>, which is representative of an inactive Neurofibromin protein. In the closed conformation, both sets of the GRD and Sec14-PH domains are rotated in a way that they are inaccessible and inactive due to a <scene name='90/904315/Catalytic_triade/2'>triade</scene> consisting of residues Cysteine 1032, Histidine 1558, and Histidine 1576 that form a transition metal-binding site with zinc. The close proximity of the C1032, H1558, and H1576 residues that form the <scene name='90/904316/Closed_triade/3'>triade in closed conformation</scene> keep the GRD domain packed tightly on top of the Neurofibromin core. This tight compaction leads to steric inhibition when Neurofibromin tries to perform its function and associate with Ras. The association between Ras and Neurofibromin is supposed to occur via an <scene name='90/904316/Arg_finger/2'>Arginine finger</scene> located at Residue 1276. However, the steric hindrance from the Neurofibromin core in the closed conformation inhibits this association. Therefore, when Neurofibromin is in the closed conformation, there is no association with Ras and cell growth and proliferation is able to occur.

=== Open Conformation ===

Sandbox Reserved 1710: Difference between revisions

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 === Closed Conformation ===
-The first conformation of Neurofibromin is known as the <scene name='90/904315/Closed/2'>Closed Conformation</scene>, which is representative of an inactive Neurofibromin protein. In the closed conformation, both sets of the GRD and Sec14-PH domains are rotated in a way that they are inaccessible and inactive due to a <scene name='90/904315/Catalytic_triade/2'>triade</scene> consisting of residues Cysteine 1032, Histidine 1558, and Histidine 1576 that form a transition metal-binding site with zinc. The close proximity of the C1032, H1558, and H1576 residues that form the <scene name='90/904316/Closed_triade/1'>triade in the closed conformation</scene> keep the GRD domain packed tightly on top of the Neurofibromin core. This tight compaction leads to steric inhibition when Neurofibromin tries to perform its function and associate with Ras. The association between Ras and Neurofibromin is supposed to occur via an <scene name='90/904316/Arg_finger/2'>Arginine finger</scene> located at Residue 1276. However, the steric hindrance from the Neurofibromin core in the closed conformation inhibits this association. Therefore, when Neurofibromin is in the closed conformation, there is no association with Ras and cell growth and proliferation is able to occur.
+The first conformation of Neurofibromin is known as the <scene name='90/904315/Closed/2'>Closed Conformation</scene>, which is representative of an inactive Neurofibromin protein. In the closed conformation, both sets of the GRD and Sec14-PH domains are rotated in a way that they are inaccessible and inactive due to a <scene name='90/904315/Catalytic_triade/2'>triade</scene> consisting of residues Cysteine 1032, Histidine 1558, and Histidine 1576 that form a transition metal-binding site with zinc. The close proximity of the C1032, H1558, and H1576 residues that form the <scene name='90/904316/Closed_triade/3'>triade in closed conformation</scene> keep the GRD domain packed tightly on top of the Neurofibromin core. This tight compaction leads to steric inhibition when Neurofibromin tries to perform its function and associate with Ras. The association between Ras and Neurofibromin is supposed to occur via an <scene name='90/904316/Arg_finger/2'>Arginine finger</scene> located at Residue 1276. However, the steric hindrance from the Neurofibromin core in the closed conformation inhibits this association. Therefore, when Neurofibromin is in the closed conformation, there is no association with Ras and cell growth and proliferation is able to occur.
 === Open Conformation ===