Sandbox Reserved 707: Difference between revisions

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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 activation segment 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/>

Sandbox Reserved 707: Difference between revisions

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Revision as of 16:36, 5 January 2013 view source Gilles A. Dupouy (talk \| contribs) 114 edits No edit summary ← Older edit		Revision as of 16:46, 5 January 2013 view source Gilles A. Dupouy (talk \| contribs) 114 edits No edit summary Newer edit →
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	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 activation segment 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/>