Sandbox Reserved 707: Difference between revisions
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'''1.''' The open form allows access of ATP and release of ADP from the active site.<br /> | '''1.''' The open form allows access of ATP and release of ADP from the active site.<br /> | ||
'''2.''' The closed form brings the residues of the substrate into the active site.<br /> | '''2.''' The closed form brings the residues of the substrate into the active site.<br /> | ||
On the other hand each lobe has her proper polypeptide segment that can change conformation from active to inactive and vice versa.<br /> | |||
On the other hand each lobe has her proper polypeptide segment that can change conformation from active to inactive and vice versa.<br /> | |||
'''1.''' In the small lobe, this segment is a α-helix, which is called αC-helix. The αC-helix rotates and translates with respect to the rest of the lobe, making or breaking part of the active site.<br /> | '''1.''' In the small lobe, this segment is a α-helix, which is called αC-helix. The αC-helix rotates and translates with respect to the rest of the lobe, making or breaking part of the active site.<br /> | ||
'''2.''' In the large lobe, the activation segment can make or break part of the ATP binding site<ref>PMID:3291115</ref>.<br /> | '''2.''' In the large lobe, the activation segment can make or break part of the ATP binding site<ref>PMID:3291115</ref>.<br /> | ||
The activation segment of each protein kinase has a specific domain that begins with a DFG amino acid sequence that can easily change its conformation (active or inactive conformation). In the inactive conformation<ref>PMID:19276351</ref> the phenylalanine side chain occupies the ATP binding pocket and the aspartate side chain faces away from the active site. This is the DFG Aspartate '''Out''' Conformation. In the active conformation, the phenylalanine side chain is rotated out of the ATP binding pocket and the Aspartate side chain can now face the ATP binding pocket and form coordinated links with the Mg²⁺. This is called the DFG Aspartate '''In''' Conformation. The activation segment can be phosphorylated by members of the same protein kinase family or by other protein kinases. <br /> | The activation segment of each protein kinase has a specific domain that begins with a DFG amino acid sequence that can easily change its conformation (active or inactive conformation). In the inactive conformation<ref>PMID:19276351</ref> the phenylalanine side chain occupies the ATP binding pocket and the aspartate side chain faces away from the active site. This is the DFG Aspartate '''Out''' Conformation. In the active conformation, the phenylalanine side chain is rotated out of the ATP binding pocket and the Aspartate side chain can now face the ATP binding pocket and form coordinated links with the Mg²⁺. This is called the DFG Aspartate '''In''' Conformation. The activation segment can be phosphorylated by members of the same protein kinase family or by other protein kinases. <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 /> | 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 /> | ||
