Sandbox Reserved 707: Difference between revisions

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As all RAF Proteins, B-RAF has the characteristic <scene name='Sandbox_Reserved_707/Small_lobe/1'>small N-terminal lobe</scene> and the <scene name='Sandbox_Reserved_707/Large_lobe/1'>large C-terminal lobe</scene>.

The small lobe is constituted of an antiparallel β-shift that anchors and orient the ATP. It contains a glycine rich ATP phosphate binding loop, called <scene name='Sandbox_Reserved_707/Glycine_rich_loop/1'>P-loop</scene>. The large lobe interacts with the substrate that in our case is MEK1/2 who needs to be phosphorylated to be active. The <scene name='Sandbox_Reserved_707/Active_site_of_1uwh/1'>catalytic site</scene> is just between the two lobes. These 2 lobes can move relative to each other, opening or closing the cleft. This has 2 major consequences on the functioning of this enzyme:<br />

The small lobe is constituted of an antiparallel β-shift that anchors and orient the ATP. It contains a glycine rich ATP phosphate binding loop, called <scene name='Sandbox_Reserved_707/Glycine_rich_loop/1'>P-loop</scene>. The large lobe interacts with the substrate that in our case is MEK1/2 who needs to be phosphorylated to be active. The <scene name='Sandbox_Reserved_707/Active_site_of_1uwh/1'>catalytic site</scene><ref>PMID:3291115</ref> is just between the two lobes. These 2 lobes can move relative to each other, opening or closing the cleft. This has 2 major consequences on the functioning of this enzyme:<br />

'''1.''' The open form allows access of ATP and release of ADP from the active site.<br />

Sandbox Reserved 707: Difference between revisions

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 As all RAF Proteins, B-RAF has the characteristic <scene name='Sandbox_Reserved_707/Small_lobe/1'>small N-terminal lobe</scene> and the <scene name='Sandbox_Reserved_707/Large_lobe/1'>large C-terminal lobe</scene>.
-The small lobe is constituted of an antiparallel β-shift that anchors and orient the ATP. It contains a glycine rich ATP phosphate binding loop, called <scene name='Sandbox_Reserved_707/Glycine_rich_loop/1'>P-loop</scene>. The large lobe interacts with the substrate that in our case is MEK1/2 who needs to be phosphorylated to be active. The <scene name='Sandbox_Reserved_707/Active_site_of_1uwh/1'>catalytic site</scene> is just between the two lobes. These 2 lobes can move relative to each other, opening or closing the cleft. This has 2 major consequences on the functioning of this enzyme:<br />
+The small lobe is constituted of an antiparallel β-shift that anchors and orient the ATP. It contains a glycine rich ATP phosphate binding loop, called <scene name='Sandbox_Reserved_707/Glycine_rich_loop/1'>P-loop</scene>. The large lobe interacts with the substrate that in our case is MEK1/2 who needs to be phosphorylated to be active. The <scene name='Sandbox_Reserved_707/Active_site_of_1uwh/1'>catalytic site</scene><ref>PMID:3291115</ref> is just between the two lobes. These 2 lobes can move relative to each other, opening or closing the cleft. This has 2 major consequences on the functioning of this enzyme:<br />
 <Structure load='1UWH' size='400' frame='true' align='left' caption='3D View of the complex ; resolution 2,95 A' scene='Insert optional scene name here' />
 '''1.'''     The open form allows access of ATP and release of ADP from the active site.<br />