Neurofibromin: Difference between revisions

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====Ras binding site====

<scene name='90/904325/Ras_and_arg_finger_binding/1'>Ras and Neurofibromin</scene>associate through the arginine finger, 1276 that comes from neurofibromin. This arginine is referred to as the [http://https://en.wikipedia.org/wiki/Arginine_finger “arginine finger”] and assists in the hydrolysis of GTP by binding to a backbone carbon atom of tyrosine 32 of Ras when neurofibromin is in the open conformation. It points into the <scene name='90/904326/Active_site_with_residues/7'>GTP binding site</scene> of Ras when neurofibromin is in the open conformation. R1276 also helps stabilize the position of Glutamine 61, a key catalytic residue, through hydrogen bonds, as well as GTP.

<scene name='90/904325/Ras_and_arg_finger_binding/2'>Ras and Neurofibromin</scene>associate through the arginine finger, 1276 that comes from neurofibromin. This arginine is referred to as the [http://https://en.wikipedia.org/wiki/Arginine_finger “arginine finger”] and assists in the hydrolysis of GTP by binding to a backbone carbon atom of tyrosine 32 of Ras when neurofibromin is in the open conformation. It points into the <scene name='90/904326/Active_site_with_residues/7'>GTP binding site</scene> of Ras when neurofibromin is in the open conformation. R1276 also helps stabilize the position of Glutamine 61, a key catalytic residue, through hydrogen bonds, as well as GTP.

Glutamine 61 of Ras is a residue that facilitates the conversion of GTP to GDP, turning Ras from its active state to inactive state. There is a catalytic water molecule that glutamine interacts with to position the molecule for a nucleophilic attack on the gamma phosphate of GTP. Mutations of this residue have been related to lower rates of hydrolysis. <ref name= ''Frech''>PMID:8136358</ref>. Tyrosine 32 makes water-mediated hydrogen bonds with the gamma phosphate of GTP. This position is also where Ras is phosphorylation to promote the activity of GTPase-activating proteins and GTP hydrolysis. <ref name= ''Bunda''>DOI:10.1038/ncomms9859</ref>

Neurofibromin: Difference between revisions

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 ====Ras binding site====
-<scene name='90/904325/Ras_and_arg_finger_binding/1'>Ras and Neurofibromin</scene>associate through the arginine finger, 1276 that comes from neurofibromin. This arginine is referred to as the [http://https://en.wikipedia.org/wiki/Arginine_finger “arginine finger”] and assists in the hydrolysis of GTP by binding to a backbone carbon atom of tyrosine 32 of Ras when neurofibromin is in the open conformation. It points into the <scene name='90/904326/Active_site_with_residues/7'>GTP binding site</scene> of Ras when neurofibromin is in the open conformation. R1276 also helps stabilize the position of Glutamine 61, a key catalytic residue, through hydrogen bonds, as well as GTP.
+<scene name='90/904325/Ras_and_arg_finger_binding/2'>Ras and Neurofibromin</scene>associate through the arginine finger, 1276 that comes from neurofibromin. This arginine is referred to as the [http://https://en.wikipedia.org/wiki/Arginine_finger “arginine finger”] and assists in the hydrolysis of GTP by binding to a backbone carbon atom of tyrosine 32 of Ras when neurofibromin is in the open conformation. It points into the <scene name='90/904326/Active_site_with_residues/7'>GTP binding site</scene> of Ras when neurofibromin is in the open conformation. R1276 also helps stabilize the position of Glutamine 61, a key catalytic residue, through hydrogen bonds, as well as GTP.
 Glutamine 61 of Ras is a residue that facilitates the conversion of GTP to GDP, turning Ras from its active state to inactive state. There is a catalytic water molecule that glutamine interacts with to position the molecule for a nucleophilic attack on the gamma phosphate of GTP. Mutations of this residue have been related to lower rates of hydrolysis. <ref name= ''Frech''>PMID:8136358</ref>. Tyrosine 32 makes water-mediated hydrogen bonds with the gamma phosphate of GTP. This position is also where Ras is phosphorylation to promote the activity of GTPase-activating proteins and GTP hydrolysis. <ref name= ''Bunda''>DOI:10.1038/ncomms9859</ref>