Neurofibromin: Difference between revisions

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The N-HEAT/ARM and C-HEAT/ARM are rigid, which makes them critical in the rearrangement of the Gap-related and Sec14-PH domains. In the closed conformation, the HEAT/ARM domains cover the GRD, preventing the binding of Ras through steric hinderance. The HEAT/ARM cores are made up of many alpha helices. <ref>DOI 10.1038/s41594-021-00687-2</ref>

==== GRD domain ====

The Gap-related domain, or GRD, is the catalytic domain of neurofibromin. This domain also contains a tubulin-binding domain. Its main catalytic mechanism is the hydrolysis of GTP-bound Ras into GDP-bound Ras, which converts Ras from its active form into its inactive form. The GRD provides an arginine residue, known as the arginine finger, to Ras. The location of the Gap-related domain is shifted between the <scene name='90/904326/Open_conformation_with_grd_hig/3'>~~grd~~ open </scene> and <scene name='90/904326/Grd_closed_conformation/3'>closed</scene> conformations of neurofibromin.

The Gap-related domain, or GRD, is the catalytic domain of neurofibromin. This domain also contains a tubulin-binding domain. Its main catalytic mechanism is the hydrolysis of GTP-bound Ras into GDP-bound Ras, which converts Ras from its active form into its inactive form. The GRD provides an arginine residue, known as the arginine finger, to Ras. The location of the Gap-related domain is shifted between the <scene name='90/904326/Open_conformation_with_grd_hig/3'>open </scene> and <scene name='90/904326/Grd_closed_conformation/3'>closed</scene> conformations of neurofibromin.

==== SEC-PH ====

The Sec-PH domain is the lipid-binding domain of neurofibromin. In the <scene name='90/904326/Sec14ph_and_grd_closed/4'>closed conformation</scene> of neurofibromin, the hydrophobic core is blocked by the Gap-related domain. The <scene name='90/904326/Sec15ph_and_grd_open/4'>open conformation</scene> allows the hydrophobic core in the Sec cavity to be accessible and exposed.

Neurofibromin: Difference between revisions

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 The N-HEAT/ARM and C-HEAT/ARM are rigid, which makes them critical in the rearrangement of the Gap-related and Sec14-PH domains. In the closed conformation, the HEAT/ARM domains cover the GRD, preventing the binding of Ras through steric hinderance. The HEAT/ARM cores are made up of many alpha helices. <ref>DOI 10.1038/s41594-021-00687-2</ref>
 ==== GRD domain ====
-The Gap-related domain, or GRD, is the catalytic domain of neurofibromin. This domain also contains a tubulin-binding domain. Its main catalytic mechanism is the hydrolysis of GTP-bound Ras into GDP-bound Ras, which converts Ras from its active form into its inactive form. The GRD provides an arginine residue, known as the arginine finger, to Ras. The location of the Gap-related domain is shifted between the <scene name='90/904326/Open_conformation_with_grd_hig/3'>grd open </scene> and <scene name='90/904326/Grd_closed_conformation/3'>closed</scene> conformations of neurofibromin.
+The Gap-related domain, or GRD, is the catalytic domain of neurofibromin. This domain also contains a tubulin-binding domain. Its main catalytic mechanism is the hydrolysis of GTP-bound Ras into GDP-bound Ras, which converts Ras from its active form into its inactive form. The GRD provides an arginine residue, known as the arginine finger, to Ras. The location of the Gap-related domain is shifted between the <scene name='90/904326/Open_conformation_with_grd_hig/3'>open </scene> and <scene name='90/904326/Grd_closed_conformation/3'>closed</scene> conformations of neurofibromin.
 ==== SEC-PH ====
 The Sec-PH domain is the lipid-binding domain of neurofibromin. In the <scene name='90/904326/Sec14ph_and_grd_closed/4'>closed conformation</scene> of neurofibromin, the hydrophobic core is blocked by the Gap-related domain. The <scene name='90/904326/Sec15ph_and_grd_open/4'>open conformation</scene> allows the hydrophobic core in the Sec cavity to be accessible and exposed.