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1lin
From Proteopedia
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(New page: 200px<br /><applet load="1lin" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lin, resolution 2.0Å" /> '''CALMODULIN COMPLEXED ...)
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Revision as of 18:28, 20 November 2007
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CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)
Overview
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.
About this Structure
1LIN is a Single protein structure of sequence from Bos taurus with CA and TFP as ligands. Full crystallographic information is available from OCA.
Reference
Trifluoperazine-induced conformational change in Ca(2+)-calmodulin., Vandonselaar M, Hickie RA, Quail JW, Delbaere LT, Nat Struct Biol. 1994 Nov;1(11):795-801. PMID:7634090
Page seeded by OCA on Tue Nov 20 20:35:15 2007
