Sandbox Reserved 826: Difference between revisions
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== '''CDK4 structure''' == | == '''CDK4 structure''' == | ||
In order to gain structural information about CDKs, a crystallographic analysis of CDK in complex with cyclin D was performed. CDK4 and cyclin D1, were overexpressed in insect cells for crystallisation and slightly modified for better crystallization. CDK 4 possesses the typical <scene name='56/568024/Bilobal_cdk4/1'>bilobal structure</scene> of kinases, containing a 5-strandet ß-sheet and a N-terminal domain (residues 1-96). Within the N-terminal domain the helix alpha-C is packed against the ß-sheet. Furthermore an ATP binding site is located in between these domains, which might bind ATP after minimal conformational rearrangement of residues Asp-99, Asp-140, Lys-142, and Tyr-17. Residues 161-171 form a <scene name='56/568024/T_loop/1'>T loop</scene> containing alpha-helices. Phosphorylation of this T-loop on residue Thr-172 or cyclin D binding may change its conformation in order to activate kinase activity of CDK4. Lambda-phosphatase incubation studies confirm the importance of phosphorylation of the T-loop for full kinase activity <ref> PMID: 19237565 </ref>. | In order to gain structural information about CDKs, a crystallographic analysis of CDK in complex with cyclin D was performed. CDK4 and cyclin D1, were overexpressed in insect cells for crystallisation and slightly modified for better crystallization. CDK 4 possesses the typical <scene name='56/568024/Bilobal_cdk4/1'>bilobal structure</scene> of kinases, containing a 5-strandet ß-sheet and a N-terminal domain (residues 1-96). Within the N-terminal domain the helix alpha-C is packed against the ß-sheet. Furthermore an ATP binding site is located in between these domains, which might bind ATP after minimal conformational rearrangement of residues Asp-99, Asp-140, Lys-142, and Tyr-17. Residues 161-171 form a <scene name='56/568024/T_loop/1'>T loop</scene> containing alpha-helices. Phosphorylation of this T-loop on residue Thr-172 or cyclin D binding may change its conformation in order to activate kinase activity of CDK4. Lambda-phosphatase incubation studies confirm the importance of phosphorylation of the T-loop for full kinase activity <ref> PMID: 19237565 </ref>. | ||
<Structure load='56/568024/Cyclin_d1/1' size='300' frame='true' align='right' caption='3D structure of cyclin D1 helices' scene='Insert optional scene name here' /> | |||
== '''Cyclin D1 structure''' == | == '''Cyclin D1 structure''' == | ||