1lin: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1lin.gif|left|200px]]
-<!--
+==CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)==
-The line below this paragraph, containing "STRUCTURE_1lin", creates the "Structure Box" on the page.
+<StructureSection load='1lin' size='340' side='right'caption='[[1lin]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1lin]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1LIN FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
-{{STRUCTURE_1lin|  PDB=1lin  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lin OCA], [https://pdbe.org/1lin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lin RCSB], [https://www.ebi.ac.uk/pdbsum/1lin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lin ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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).
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/li/1lin_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lin ConSurf].
+<div style="clear:both"></div>
-'''CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)'''
+==See Also==
+*[[Calmodulin 3D structures|Calmodulin 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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==
-LIN 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==
-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: Single protein]]
+[[Category: Large Structures]]
-[[Category: Delbaere, L T.J.]]
+[[Category: Delbaere LTJ]]
-[[Category: Hickie, R A.]]
+[[Category: Hickie RA]]
-[[Category: Quail, J W.]]
+[[Category: Quail JW]]
-[[Category: Vandonselaar, M.]]
+[[Category: Vandonselaar M]]
-[[Category: Calcium-binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 23:57:27 2008''