Neurofibromin: Difference between revisions
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[[Image:Nfdomains2.png|800 px|thumb|Figure 1. Domains of Neurofibromin.]] | [[Image:Nfdomains2.png|800 px|thumb|Figure 1. Domains of Neurofibromin.]] | ||
==== GRD domain ==== | ==== 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 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. | ||
==== SEC-PH ==== | ==== SEC-PH ==== | ||
The Sec-PH domain is the lipid-binding domain of neurofibromin. In the <scene name='90/904326/Sec14ph_and_grd_closed/2'>closed conformation</scene> of neurofibromin, the hydrophobic core is blocked by the Gap-related domain. The <scene name='90/904326/Sec15ph_and_grd_open/2'>open conformation</scene> allows the hydrophobic core in the Sec cavity to be accessible and exposed. | The Sec-PH domain is the lipid-binding domain of neurofibromin. In the <scene name='90/904326/Sec14ph_and_grd_closed/2'>closed conformation</scene> of neurofibromin, the hydrophobic core is blocked by the Gap-related domain. The <scene name='90/904326/Sec15ph_and_grd_open/2'>open conformation</scene> allows the hydrophobic core in the Sec cavity to be accessible and exposed. | ||
