Solution Structure of 21-Residue Peptide (Asp 84-Leu 104), Functional Site derived from <TEX>$p16^{INK4A}$</TEX>

Lee, Ho-Jin; 이호진; Ahn, In-Ae; 안인애; Ro, Seonggu; 노성구; Choi, Young-Sang; 최영상; Yoon, Chang No; 윤창노; Lee, Kang-Bong; 이강봉

오늘 하루 그만보기

P-ISSN1225-0163
E-ISSN2288-8985
SCOPUS, ESCI, KCI

Home

Browse Articles

Article Detail

Home > Article Detail

P-ISSN 1225-0163
E-ISSN 2288-8985

e-Submission

Vol.13, No.4

PubReader Citation

Solution Structure of 21-Residue Peptide (Asp 84-Leu 104), Functional Site derived from $p16^{INK4A}$

Analytical Science and Technology / Analytical Science and Technology, (P)1225-0163; (E)2288-8985

2000, v.13 no.4, pp.494-503

Lee, Ho-Jin
Ahn, In-Ae
Ro, Seonggu
Choi, Young-Sang
Yoon, Chang No
Lee, Kang-Bong

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>, 13(4), 494-503.

copy

Abstract

A 21-residue peptide corresponding to amino acids 84-104 of $p16^{INK4A}$, the tumor suppressor, has been synthesized and its structure was studied by Circular Dichroism, $^1H$ 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, $^3J_{NH-H{\alpha}}$ coupling constants, $C_{\alpha}H$ 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 ${\gamma}$-turn conformation between residues $Gly^{89}-Leu^{91}$(${\varphi}_{i+1}