1lin
From Proteopedia
(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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| - | [[Image:1lin.gif|left|200px]]<br /><applet load="1lin" size=" | + | [[Image:1lin.gif|left|200px]]<br /><applet load="1lin" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lin, resolution 2.0Å" /> | caption="1lin, resolution 2.0Å" /> | ||
'''CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)'''<br /> | '''CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Here we show that, as a consequence of binding the drug trifluoperazine, a | + | 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== | ==About this Structure== | ||
| - | 1LIN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA and TFP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1LIN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=TFP:'>TFP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LIN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Delbaere, L | + | [[Category: Delbaere, L T.J.]] |
| - | [[Category: Hickie, R | + | [[Category: Hickie, R A.]] |
| - | [[Category: Quail, J | + | [[Category: Quail, J W.]] |
[[Category: Vandonselaar, M.]] | [[Category: Vandonselaar, M.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:17 2008'' |
Revision as of 11:45, 21 February 2008
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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 and 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
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