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- E-ISSN 2288-8985
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Solution Structure of 21-Residue Peptide (Asp 84-Leu 104), Functional Site derived from <TEX>$p16^{INK4A}$</TEX>
Analytical Science and Technology / Analytical Science and Technology, (P)1225-0163; (E)2288-8985
2000, v.13 no.4, pp.494-503
Lee,
H., Ahn,
I., Ro,
S., Choi,
Y., Yoon,
C. N., &
Lee,
K.
(2000). Solution Structure of 21-Residue Peptide (Asp 84-Leu 104), Functional Site derived from <TEX>$p16^{INK4A}$</TEX>. Analytical Science and Technology, 13(4), 494-503.
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Abstract
A 21-residue peptide corresponding to amino acids 84-104 of <TEX>$p16^{INK4A}$</TEX>, the tumor suppressor, has been synthesized and its structure was studied by Circular Dichroism, <TEX>$^1H$</TEX> NMR spectroscopy and molecular modeling. A p16-derived peptide (84-104 amino acids) forming stable complex with CDK4 and CDK6 inhibits the ability of CDK4/6 to phosphorylate pRb in vitro, and blocks cell-cycle progression through G1/S phase as shown in the function of the full-length p16. Its NMR spectral data including NOEs, <TEX>$^3J_{NH-H{\alpha}}$</TEX> coupling constants, <TEX>$C_{\alpha}H$</TEX> chemical shift, the average amplitude of amide chemical shift oscillation and temperature coefficients indicate that the secondary structure of a p16-derived peptide is similar to that of the same region of full-length p16, which consists of helix-turn-helix structure. The 3-D distance geometry structure based on NOE-hased distance and torsion angle restraints is characterized by <TEX>${\gamma}$</TEX>-turn conformation between residues <TEX>$Gly^{89}-Leu^{91}$</TEX>(<TEX>${\varphi}_{i+1}
- keywords
- <TEX>$p16^{INK4A}$</TEX>, <TEX>$^IH$</TEX> NMR, distance geometry, peptide, <TEX>${\gamma}$</TEX>-turn, three-dimensional structure
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