This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1lin
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1lin.gif|left|200px]] | + | [[Image:1lin.gif|left|200px]] |
| - | + | ||
| - | '''CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)''' | + | {{Structure |
| + | |PDB= 1lin |SIZE=350|CAPTION= <scene name='initialview01'>1lin</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=TFP:10-[3-(4-METHYL-PIPERAZIN-1-YL)-PROPYL]-2-TRIFLUOROMETHYL-10H-PHENOTHIAZINE'>TFP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1LIN is a [ | + | 1LIN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LIN OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7634090 7634090] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 21: | Line 30: | ||
[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:31:20 2008'' |
Revision as of 10:31, 20 March 2008
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 12:31:20 2008
