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NMR structural characterization of the CDK inhibitor p19 INK4d
Author(s) -
Kalus Wenzel,
Baumgartner Roland,
Renner Christian,
Noegel Angelika,
Chan Francis Ka Ming,
Winoto Astar,
Holak Tad A
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01465-2
Subject(s) - ankyrin repeat , helix (gastropod) , ankyrin , protein secondary structure , heteronuclear molecule , protein structure , chemistry , circular dichroism , stereochemistry , alpha helix , crystallography , biology , biochemistry , nuclear magnetic resonance spectroscopy , ecology , snail , gene
p19 INK4d is a 165 amino acid protein that belongs to the INK4 family of CDK4 and CDK6 inhibitors. Assignments of 1 H, 15 N and 13 C 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 . 1 H‐ 15 N 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.