Neurofibromin: Difference between revisions

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===Domains===
===Domains===
Neurofibromin consists of multiple domains: N-HEAT/ARM, GRD, Sec14-PH, GAPEx, and C-HEAT/ARM. The two most characterized domains of neurofibromin are the Sec14-PH and GRD domains. Each of the protomers of neurofibromin contains these domains.  
Neurofibromin consists of multiple domains: N-HEAT/ARM, GRD, Sec14-PH, GAPEx, and C-HEAT/ARM. The two most characterized domains of neurofibromin are the Sec14-PH and GRD domains. Each of the protomers of neurofibromin contains these domains.  
[[Image:domainsneurofibromin.png|800 px|thumb|Figure 1. Domains of Neurofibromin.]]
[[Image:domainsneurofibromin.png|700 px|thumb|Figure 1. Domains of Neurofibromin.]]
====N-HEAT/ARM and C-HEAT/ARM====
====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: [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>
[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>
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