1ZZ2

Two Classes of p38alpha MAP Kinase Inhibitors Having a Common Diphenylether Core but Exhibiting Divergent Binding Modes

1ZZ2 の概要

• エントリーDOI: 10.2210/pdb1zz2/pdb
• 関連するPDBエントリー: 1ZYJ
• 分子名称: Mitogen-activated protein kinase 14, octyl beta-D-glucopyranoside, N-[3-(4-FLUOROPHENOXY)PHENYL]-4-[(2-HYDROXYBENZYL)AMINO]PIPERIDINE-1-SULFONAMIDE, ... (4 entities in total)
• 機能のキーワード: protein-inhibitor complex, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm (By similarity): Q16539
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42107.11

構造登録者

Michelotti, E.L.,Moffett, K.K.,Springman, E.B.,Karpusas, M. (登録日: 2005-06-13, 公開日: 2005-10-18, 最終更新日: 2024-02-14)

主引用文献

Michelotti, E.L.,Moffett, K.K.,Nguyen, D.,Kelly, M.J.,Shetty, R.,Chai, X.,Northrop, K.,Namboodiri, V.,Campbell, B.,Flynn, G.A.,Fujimoto, T.,Hollinger, F.P.,Bukhtiyarova, M.,Springman, E.B.,Karpusas, M.
Two classes of p38alpha MAP kinase inhibitors having a common diphenylether core but exhibiting divergent binding modes.
Bioorg.Med.Chem.Lett., 15:5274-5279, 2005

PubMed Abstract: Two new classes of diphenylether inhibitors of p38alpha MAP kinase are described. Both chemical classes are based on a common diphenylether core that is identified by simulated fragment annealing as one of the most favored chemotypes within a prominent hydrophobic pocket of the p38alpha ATP-binding site. In the fully elaborated molecules, the diphenylether moiety acts as an anchor occupying the deep pocket, while polar extensions make specific interactions with either the adenine binding site or the phosphate binding site of ATP. The synthesis, crystallographic analysis, and biological activity of these p38alpha inhibitors are discussed.

PubMed: 16169718
DOI: 10.1016/j.bmcl.2005.08.038

実験手法

X-RAY DIFFRACTION (2 Å)