Neurofibromin: Difference between revisions

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[[Image:domainsneurofibromin.png|800 px|thumb|Figure 1. Domains of Neurofibromin.]]

====N-HEAT/ARM and C-HEAT/ARM====

[https://en.wikipedia.org/wiki/HEAT_repeat Heat domains] are domains found in cytoplasmic proteins that consist of four different proteins: Huntingtin, elongation factor 3, protein phosphatase 2A, and TOR1. <ref name= ''Yoshimura''>DOI: 10.1242/jcs.185710</ref>. The HEAT/ARM cores are made up of many alpha helices. 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. <ref>DOI 10.1038/s41594-021-00687-2</ref>

[https://en.wikipedia.org/wiki/HEAT_repeat Heat domains] are domains found in cytoplasmic proteins that consist of four different proteins: [https://proteopedia.org/wiki/index.php/Huntingtin Huntingtin], [https://proteopedia.org/wiki/index.php/Elongation_factor elongation factor 3], [https://proteopedia.org/wiki/index.php/Protein_phosphatase protein phosphatase 2A], and TOR1. <ref name= ''Yoshimura''>DOI: 10.1242/jcs.185710</ref>. The HEAT/ARM cores are made up of many alpha helices. 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. <ref>DOI 10.1038/s41594-021-00687-2</ref>

==== GRD domain ====

The Gap-related domain, or GRD, is the catalytic domain of neurofibromin. It ranges from residues 1196 to 1547. <ref>DOI 10.1038/s41586-021-04024-x</ref> 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.

Neurofibromin: Difference between revisions

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@@ Line 8: / Line 8: @@
 [[Image:domainsneurofibromin.png|800 px|thumb|Figure 1. Domains of Neurofibromin.]]
 ====N-HEAT/ARM and C-HEAT/ARM====
-[https://en.wikipedia.org/wiki/HEAT_repeat Heat domains] are domains found in cytoplasmic proteins that consist of four different proteins: Huntingtin, elongation factor 3, protein phosphatase 2A, and TOR1. <ref name= ''Yoshimura''>DOI: 10.1242/jcs.185710</ref>. The HEAT/ARM cores are made up of many alpha helices. 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. <ref>DOI 10.1038/s41594-021-00687-2</ref>
+[https://en.wikipedia.org/wiki/HEAT_repeat Heat domains] are domains found in cytoplasmic proteins that consist of four different proteins: [https://proteopedia.org/wiki/index.php/Huntingtin Huntingtin], [https://proteopedia.org/wiki/index.php/Elongation_factor elongation factor 3], [https://proteopedia.org/wiki/index.php/Protein_phosphatase protein phosphatase 2A], and TOR1. <ref name= ''Yoshimura''>DOI: 10.1242/jcs.185710</ref>. The HEAT/ARM cores are made up of many alpha helices. 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. <ref>DOI 10.1038/s41594-021-00687-2</ref>
 ==== GRD domain ====
 The Gap-related domain, or GRD, is the catalytic domain of neurofibromin. It ranges from residues 1196 to 1547. <ref>DOI 10.1038/s41586-021-04024-x</ref> 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.