1lin

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[[Image:1lin.gif|left|200px]]
[[Image:1lin.gif|left|200px]]
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{{Structure
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|PDB= 1lin |SIZE=350|CAPTION= <scene name='initialview01'>1lin</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1lin", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TFP:10-[3-(4-METHYL-PIPERAZIN-1-YL)-PROPYL]-2-TRIFLUOROMETHYL-10H-PHENOTHIAZINE'>TFP</scene>
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{{STRUCTURE_1lin| PDB=1lin | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lin OCA], [http://www.ebi.ac.uk/pdbsum/1lin PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lin RCSB]</span>
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'''CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)'''
'''CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)'''
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[[Category: Quail, J W.]]
[[Category: Quail, J W.]]
[[Category: Vandonselaar, M.]]
[[Category: Vandonselaar, M.]]
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[[Category: calcium-binding protein]]
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[[Category: Calcium-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:57:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:03:14 2008''
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Revision as of 20:57, 2 May 2008

Image:1lin.gif

Template:STRUCTURE 1lin

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. 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 Fri May 2 23:57:27 2008

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