NMR structural characterization of the CDK inhibitor p19INK4d

FEBS Letters

Renner, Christian²  Noegel, Angelika²  Holak, Tad A²  Chan, Francis Ka Ming¹  Kalus, Wenzel²  Baumgartner, Roland²  Winoto, Astar¹ 

[1] Department of Molecular and Cell Biology, 469 Life Science Addition, University of California, Berkeley, CA 94720-3200, USA;Max Planck Institute for Biochemistry, D-82152 Martinsried, Germany

关键词: p19;    CDK inhibitor;    Ankyrin repeat;    INK4;    Nuclear magnetic resonance;   

DOI  :  10.1016/S0014-5793(96)01465-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

p19^INK4d is a 165 amino acid protein that belongs to the INK4 family of CDK4 and CDK6 inhibitors. Assignments of ¹H, ¹⁵N and ¹³C resonances have enabled the determination of the secondary structure of the protein which is largely α-helical (residues 14–18, 21–29, 54–62, 77–83, 87–95, 110–116, 120–128, 142–148 and 152–160). The protein comprises five 32-amino acid ankyrin-like repeats; each ankyrin repeat contains a helix-β-turn-helix core. The exception is the second ankyrin repeat, which lacks the first helix. All β-turns have a central glycine residue flanked by two residues in β-conformations. There is also a high conservation of Ala at position 8 in the first helix and Leu-Leu(Val) at positions 17–18 of the second helix in all ankyrin repeats of p19. The location of the helix-turn-helix segments found in p19 should be general for all other members of the INK4 family, including, for example, a homologous tumor suppressor p16^INK4a. ¹H-¹⁵N heteronuclear steady-state NOE measurements on p19 indicate that most of the backbone of p19^INK4d exists in a well defined structure of limited conformational flexibility on the nano- to picosecond time scale.

【 授权许可】

Unknown