1lin

<StructureSection load='1lin' size='340' side='right' caption='[[1lin]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[1lin]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LIN FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1lin PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lin RCSB], [http://www.ebi.ac.uk/pdbsum/1lin PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/CALM_BOVIN CALM_BOVIN]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CEP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (By similarity).

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/li/1lin_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:7634090</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1lin" style="background-color:#fffaf0;"></div>

*[[Calmodulin|Calmodulin]]

[[Category: Delbaere, L T.J]]

[[Category: Hickie, R A]]

[[Category: Quail, J W]]

[[Category: Vandonselaar, M]]

[[Category: Calcium-binding protein]]