Sandbox Reserved 707: Difference between revisions
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An invariant lysine (Lys578 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 (Lys578 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/> | ||
[[Image:138 page3 image1.jpg]] | [[Image:138 page3 image1.jpg|500px|thumb| Diagram of the inferred interactions between human B-RAF kinase catalytic core residues, ATP, and MEK]] | ||
This is a table of the important residues of B-RAF:<br /> | This is a table of the important residues of B-RAF:<br /> | ||
