Neurofibromin: Difference between revisions
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The two conformations that neurofibromin exists in are the open state and closed state. The conformational change of neurofibromin involves rearrangement of the domains. | The two conformations that neurofibromin exists in are the open state and closed state. The conformational change of neurofibromin involves rearrangement of the domains. | ||
=====Closed Conformation===== | =====Closed Conformation===== | ||
The <scene name='90/904326/Overview_of_domains/1'>closed state</scene> of neurofibromin has both protomers in a closed conformation, which inhibits the binding of Ras to the GRD of neurofibromin due to the HEAT/ARM core blocking the GRD. A metal binding site between the N-HEAT/ARM domain and the GRD-Sec14-PH linker stabilize the closed conformation. This site is coordinated by three residues, <scene name='90/904325/Triad/1'>C1032, H1558, and H1576,</scene> | The <scene name='90/904326/Overview_of_domains/1'>closed state</scene> of neurofibromin has both protomers in a closed conformation, which inhibits the binding of Ras to the GRD of neurofibromin due to the HEAT/ARM core blocking the GRD. A metal binding site between the N-HEAT/ARM domain and the GRD-Sec14-PH linker stabilize the closed conformation. This site is coordinated by three residues, <scene name='90/904325/Triad/1'>C1032, H1558, and H1576,</scene>. (Figure 2). This binding site is preferential for zinc- zinc has been found to stabilize the closed conformation of neurofibromin. In the absence of zinc, neurofibromin is in the open conformation. <ref name="Naschberger"/> | ||
[[Image:greenTriad.png|200 px|thumb|Figure 2. Triad of Residues that keep Neurofibromin in the Closed Conformation.]] | [[Image:greenTriad.png|200 px|thumb|Figure 2. Triad of Residues that keep Neurofibromin in the Closed Conformation.]] | ||
=====Open Conformation===== | =====Open Conformation===== | ||
