1LIN

CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)

1LIN の概要

• エントリーDOI: 10.2210/pdb1lin/pdb
• 分子名称: CALMODULIN, CALCIUM ION, 10-[3-(4-METHYL-PIPERAZIN-1-YL)-PROPYL]-2-TRIFLUOROMETHYL-10H-PHENOTHIAZINE, ... (4 entities in total)
• 機能のキーワード: calcium-binding protein
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Cytoplasm: P62157
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18511.65

構造登録者

Vandonselaar, M.,Hickie, R.A.,Quail, J.W.,Delbaere, L.T.J. (登録日: 1995-10-11, 公開日: 1996-03-08, 最終更新日: 2024-02-14)

主引用文献

Vandonselaar, M.,Hickie, R.A.,Quail, J.W.,Delbaere, L.T.
Trifluoperazine-induced conformational change in Ca(2+)-calmodulin.
Nat.Struct.Biol., 1:795-801, 1994

PubMed Abstract: Here we show that, as a consequence of binding the drug trifluoperazine, a major conformational movement occurs in Ca(2+)-calmodulin (CaM). The tertiary structure changes from an elongated dumb-bell, with exposed hydrophobic surfaces, to a compact globular form which can no longer interact with its target enzymes. It is likely that inactivation of Ca(2+)-CaM by trifluoperazine is due to this major tertiary-structural alteration in Ca(2+)-CaM, which is initiated and stabilized by drug binding. This conformational change is similar to that which occurs on the binding of Ca(2+)-CaM to target peptides. Two hydrophobic binding pockets, created by amino acid residues adjacent to Ca(2+)-coordinating residues, form the key recognition sites on Ca(2+)-CaM for both inhibitors and target enzymes.

PubMed: 7634090
DOI: 10.1038/nsb1194-795

実験手法

X-RAY DIFFRACTION (2 Å)