Sandbox Reserved 707: Difference between revisions
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A <scene name='Sandbox_Reserved_707/Gatekeeper_residue/1'>gatekeeper residue</scene> separates the adenine binding site from the hydrophobic pocket. Mutation on this residue can prevent the binding of kinase inhibitory drugs (the replacement of a threonine by a methionine for example).<br /> | A <scene name='Sandbox_Reserved_707/Gatekeeper_residue/1'>gatekeeper residue</scene> separates the adenine binding site from the hydrophobic pocket. Mutation on this residue can prevent the binding of kinase inhibitory drugs (the replacement of a threonine by a methionine for example).<br /> | ||
[[Image:1-s2.0-S0092867404002156-main page7 image1.jpg|left|400px|thumb| A. Structure of B-RAF Kinase Domain <br /> | |||
B. Schematic B-RAF Primary Structure<ref>PMID: 15035987</ref>]] | |||
It is very important to distinguish conserved amino acid residue signatures that constitute the catalytic core of the B-RAF Kinase. The catalytic properties are done by the <scene name='Sandbox_Reserved_707/Kdd_motif/1'>KDD (Lys578-Asp576-Asp594)</scene> Motif and the <scene name='Sandbox_Reserved_707/Activation_segment/1'>activation segment</scene> starts in general with a <scene name='Sandbox_Reserved_707/Dfg_start_activation_segment/1'>DFG</scene> and ends with <scene name='Sandbox_Reserved_707/Ape/1'>APE</scene>. But how the catalytic reaction is generated? | It is very important to distinguish conserved amino acid residue signatures that constitute the catalytic core of the B-RAF Kinase. The catalytic properties are done by the <scene name='Sandbox_Reserved_707/Kdd_motif/1'>KDD (Lys578-Asp576-Asp594)</scene> Motif and the <scene name='Sandbox_Reserved_707/Activation_segment/1'>activation segment</scene> starts in general with a <scene name='Sandbox_Reserved_707/Dfg_start_activation_segment/1'>DFG</scene> and ends with <scene name='Sandbox_Reserved_707/Ape/1'>APE</scene>. But how the catalytic reaction is generated? | ||
An invariant lysine (<scene name='Sandbox_Reserved_707/K578/1'>Lys578</scene> in B-RAF) forms salt bridges with the gamma phosphate of the ATP. Asp576, which is a base in the catalytic loop, orients the seryl or threonyl group of the substrate protein and takes the proton of the hydroxyl group, facilitating the attack of oxygen on the gamma phosphorus atom of MgATP. Asp594 binds Mg²⁺ which coordinates the beta and gamma phosphates of ATP. <br/> | An invariant lysine (<scene name='Sandbox_Reserved_707/K578/1'>Lys578</scene> in B-RAF) forms salt bridges with the gamma phosphate of the ATP. Asp576, which is a base in the catalytic loop, orients the seryl or threonyl group of the substrate protein and takes the proton of the hydroxyl group, facilitating the attack of oxygen on the gamma phosphorus atom of MgATP. Asp594 binds Mg²⁺ which coordinates the beta and gamma phosphates of ATP. <br/> | ||
This is a table of the important residues of B-RAF:<br /> | This is a table of the important residues of B-RAF:<br /> | ||
