Sandbox 210: Difference between revisions
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The activator protein of CDK5, p25, presents a cyclin-box fold domain, which is the structural motif found in the cyclins. | The activator protein of CDK5, p25, presents a cyclin-box fold domain, which is the structural motif found in the cyclins. | ||
Analyses of the crystal structures of CDK5/p25 show the existence of extensive electrostatic and Van Der Waals interactions between the β sheet, and a small loop following the C helix (f-loop) of CDK5, and an helix of p25. | Analyses of the crystal structures of CDK5/p25 show the existence of extensive electrostatic and Van Der Waals interactions between the β sheet, and a small loop following the C helix (f-loop) of CDK5, and an helix of p25. | ||
During the unbinding processes between CDK5 and p25, obvious conformational changes in the C helix and the T loop are observed. The C helix, together with the loop preceding the helix (the p-loop) apparently displaces from its original location towards the p25 side. The distances between the C-alpha carbon atoms of the tip amino acid of the p-loop (Gly43) and the starting amino acid of the C helix (Ser46) before and after pulling are 14.15 Å and 7.23 Å, respectively.<ref> | During the unbinding processes between CDK5 and p25, obvious conformational changes in the C helix and the T loop are observed. The C helix, together with the loop preceding the helix (the p-loop) apparently displaces from its original location towards the p25 side. The distances between the C-alpha carbon atoms of the tip amino acid of the p-loop (Gly43) and the starting amino acid of the C helix (Ser46) before and after pulling are 14.15 Å and 7.23 Å, respectively.<ref name="premier">doi:10.1007/s00894-009-0629-4</ref> | ||
===Sequence similarities=== | ===Sequence similarities=== | ||
