1DC2

SOLUTION NMR STRUCTURE OF TUMOR SUPPRESSOR P16INK4A, 20 STRUCTURES

1DC2 の概要

• エントリーDOI: 10.2210/pdb1dc2/pdb
• 関連するPDBエントリー: 1A5E
• NMR情報: BMRB: 4526
• 分子名称: CYCLIN-DEPENDENT KINASE 4 INHIBITOR A (P16INK4A) (1 entity in total)
• 機能のキーワード: ankyrin repeat, helix-turn-helix, helix bundle, gene regulation
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16554.64

構造登録者

Byeon, I.-J.L.,Li, J.,Yuan, C.,Tsai, M.-D. (登録日: 1999-11-04, 公開日: 1999-12-23, 最終更新日: 2024-05-22)

主引用文献

Yuan, C.,Selby, T.L.,Li, J.,Byeon, I.J.,Tsai, M.D.
Tumor suppressor INK4: refinement of p16INK4A structure and determination of p15INK4B structure by comparative modeling and NMR data.
Protein Sci., 9:1120-1128, 2000

PubMed Abstract: Within the tumor suppressor protein INK4 (inhibitor of cyclin-dependent kinase 4) family, p15INK4B is the smallest and the only one whose structure has not been determined previously, probably due to the protein's conformational flexibility and instability. In this work, multidimensional NMR studies were performed on this protein. The first tertiary structure was built by comparative modeling with p16INK4A as the template, followed by restrained energy minimization with NMR constraints (NOE and H-bonds). For this purpose, the solution structure of pl6INK4A, whose quality was also limited by similar problems, was refined with additional NMR experiments conducted on an 800 MHz spectrometer and by structure-based iterative NOE assignments. The nonhelical regions showed major improvement with root-mean-square deviation (RMSD) improved from 1.23 to 0.68 A for backbone heavy atoms. The completion of p15INK4B coupled with refinement of p16INK4A made it possible to compare the structures of the four INK4 members in depth, and to compare the structures of p16INK4A in the free form and in the p16INK4A-CDK6 complex. This is an important step toward a comprehensive understanding of the precise functional roles of each INK4 member.

PubMed: 10892805

実験手法

SOLUTION NMR