Neurofibromin: Difference between revisions
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The Gap-related domain, or <scene name='90/904326/Grd_highlighted/1'>GRD</scene>, is the catalytic domain of neurofibromin. It ranges from residues 1196 to 1547. <ref name="Naschberger"/> 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/Grdopen/1'>open conformation</scene> and closed conformations of neurofibromin. | The Gap-related domain, or <scene name='90/904326/Grd_highlighted/1'>GRD</scene>, is the catalytic domain of neurofibromin. It ranges from residues 1196 to 1547. <ref name="Naschberger"/> 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/Grdopen/1'>open conformation</scene> and closed conformations of neurofibromin. | ||
==== Sec-PH ==== | ==== Sec-PH ==== | ||
The <scene name='90/ | The <scene name='90/904325/Secph_highlighted/2'>Sec14-PH</scene> domain is the lipid-binding domain of neurofibromin, found in residues 1565 to 1835. <ref name="Naschberger"/> In the closed conformation of neurofibromin, the hydrophobic core is blocked by the Gap-related domain. The <scene name='90/904326/Secopen/1'>open conformation</scene> allows the hydrophobic core in the Sec cavity to be accessible and exposed. In neurofibromin, this cavity binds [https://en.wikipedia.org/wiki/Glycerophospholipid glycerophospholipids], which can induce conformational changes. <ref>DOI 10.1016/j.febslet.2012.06.006</ref> It is unclear if the Sec14-PH domain has a role in the RasGap activity of neurofibromin. | ||
===Important Structural Features=== | ===Important Structural Features=== | ||
====Conformations==== | ====Conformations==== | ||
