Sandbox Reserved 1706: Difference between revisions

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==History==
==History==
==Function==
==Function==
NF1 is a GTPase-activation protein that binds to RAS to increase the hydrolysis of GTP to GDP. This inactivates the cell signaling of Ras until another GTP can replace the GDP from the cytosol. NF1 and Ras binding is possible in only the  <scene name='90/904311/Open_conformation/1'>open conformation</scene> of NF1. The mechanism is shown in figure 1 and displays the slow hydrolysis of GTP bound to Ras and the fast hydrolysis of GTP when bound to NF1.  
NF1 is a [https://en.wikipedia.org/wiki/GTPase-activating_protein] that binds to RAS to increase the hydrolysis of GTP to GDP. This inactivates the cell signaling of Ras until another GTP can replace the GDP from the cytosol. NF1 and Ras binding is possible in only the  <scene name='90/904311/Open_conformation/1'>open conformation</scene> of NF1. The mechanism is shown in figure 1 and displays the slow hydrolysis of GTP bound to Ras and the fast hydrolysis of GTP when bound to NF1.  
==Structure==
==Structure==
NF1 is a protein dimer that exists in a <scene name='90/904311/Closed_conformation/1'>closed</scene> and  <scene name='90/904311/Open_conformation/1'>open</scene> conformation. Each protomer contains a GRD, Sec14-PH, and a GAPex domain located on a HEAT N-C arm. Ras binds to the GRD site with Arg1276 being the critical residue for binding.  
NF1 is a protein dimer that exists in a <scene name='90/904311/Closed_conformation/1'>closed</scene> and  <scene name='90/904311/Open_conformation/1'>open</scene> conformation. Each protomer contains a GRD, Sec14-PH, and a GAPex domain located on a HEAT N-C arm. Ras binds to the GRD site with Arg1276 being the critical residue for binding.