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[[Image:1lin.gif|left|200px]]


{{Structure
==CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)==
|PDB= 1lin |SIZE=350|CAPTION= <scene name='initialview01'>1lin</scene>, resolution 2.0&Aring;
<StructureSection load='1lin' size='340' side='right'caption='[[1lin]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|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>
<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>
|ACTIVITY=  
</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>
|GENE=  
<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>
|DOMAIN=
<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>
|RELATEDENTRY=
</table>
|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>
== 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==
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==
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: 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 Sun Mar 30 22:03:14 2008''

Latest revision as of 10:33, 14 February 2024

CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)

Structural highlights

1lin is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1lin, resolution 2.00Å

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

OCA
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