Sandbox Reserved 167: Difference between revisions
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The structure of p16INK4a is tertiary with four helix-turn-helix motifs linked by three loops. <ref name="Byeon"> Byeon, I.J., Li, J., Ericson, K., Selby, T.L., Tevelev, A., Kim, H.J., O`Maille, P., Tsai, M.D. Tumor suppressor p16INK4A: determination of solution structure and analyses of its interaction with cyclin-dependent kinase 4.(1998) Mol.Cell 1: 421-431 PMID: 9660926 </ref>. | The structure of p16INK4a is tertiary with four helix-turn-helix motifs linked by three loops. <ref name="Byeon"> Byeon, I.J., Li, J., Ericson, K., Selby, T.L., Tevelev, A., Kim, H.J., O`Maille, P., Tsai, M.D. Tumor suppressor p16INK4A: determination of solution structure and analyses of its interaction with cyclin-dependent kinase 4.(1998) Mol.Cell 1: 421-431 PMID: 9660926 </ref>. | ||
Important recognition binding units have been identified on both p16INK4a and cdk4/6, including a region of 58 residues at cdk4's n terminus for the binding of p16INK4. P16INK4a is a polypeptide chain made up of 156 units, with multiple mutant chains having been synthetically derived. <ref name="Silverman"> Silverman, Robert, RPh, MM and Ridder, Dr. Rüdiger. p16INK4a Antibody. MTM Laboratories Website. http://mtmlabs.com/us/index.php/science-a-technology/p16ink4a </ref | Important recognition binding units have been identified on both p16INK4a and cdk4/6, including a region of 58 residues at cdk4's n terminus for the binding of p16INK4. P16INK4a is a polypeptide chain made up of 156 units, with multiple mutant chains having been synthetically derived. <ref name="Silverman"> Silverman, Robert, RPh, MM and Ridder, Dr. Rüdiger. p16INK4a Antibody. MTM Laboratories Website. http://mtmlabs.com/us/index.php/science-a-technology/p16ink4a </ref>. | ||
== Future Importance of P16INK4a == | == Future Importance of P16INK4a == | ||