1LIN

CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)

Summary for 1LIN

• Entry DOI: 10.2210/pdb1lin/pdb
• Descriptor: CALMODULIN, CALCIUM ION, 10-[3-(4-METHYL-PIPERAZIN-1-YL)-PROPYL]-2-TRIFLUOROMETHYL-10H-PHENOTHIAZINE, ... (4 entities in total)
• Functional Keywords: calcium-binding protein
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm: P62157
• Total number of polymer chains: 1
• Total formula weight: 18511.65

Authors

Vandonselaar, M.,Hickie, R.A.,Quail, J.W.,Delbaere, L.T.J. (deposition date: 1995-10-11, release date: 1996-03-08, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)