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[[Image:1f71.jpg|left|200px]]
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{{STRUCTURE_1f71|  PDB=1f71  |  SCENE=  }}
'''REFINED SOLUTION STRUCTURE OF CALMODULIN C-TERMINAL DOMAIN'''


==REFINED SOLUTION STRUCTURE OF CALMODULIN C-TERMINAL DOMAIN==
<StructureSection load='1f71' size='340' side='right'caption='[[1f71]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f71]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F71 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f71 OCA], [https://pdbe.org/1f71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f71 RCSB], [https://www.ebi.ac.uk/pdbsum/1f71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f71 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CALM1_XENLA CALM1_XENLA] 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.
== 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/f7/1f71_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=1f71 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
For an increasing fraction of proteins whose structures are being studied, sequence homology to known structures permits building of low resolution structural models. It is demonstrated that dipolar couplings, measured in a liquid crystalline medium, not only can validate such structural models, but also refine them. Here, experimental 1H-15N, 1Halpha-13Calpha, and 13C'-13Calpha dipolar couplings are shown to decrease the backbone rmsd between various homology models of calmodulin (CaM) and its crystal structure. Starting from a model of the Ca2+-saturated C-terminal domain of CaM, built from the structure of Ca2+-free recoverin on the basis of remote sequence homology, dipolar couplings are used to decrease the rmsd between the model and the crystal structure from 5.0 to 1.25 A. A better starting model, built from the crystal structure of Ca2+-saturated parvalbumin, decreases in rmsd from 1.25 to 0.93 A. Similarly, starting from the structure of the Ca2+-ligated CaM N-terminal domain, experimental dipolar couplings measured for the Ca2+-free form decrease the backbone rmsd relative to the refined solution structure of apo-CaM from 4.2 to 1.0 A.


==Overview==
Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings.,Chou JJ, Li S, Bax A J Biomol NMR. 2000 Nov;18(3):217-27. PMID:11142512<ref>PMID:11142512</ref>
For an increasing fraction of proteins whose structures are being studied, sequence homology to known structures permits building of low resolution structural models. It is demonstrated that dipolar couplings, measured in a liquid crystalline medium, not only can validate such structural models, but also refine them. Here, experimental 1H-15N, 1Halpha-13Calpha, and 13C'-13Calpha dipolar couplings are shown to decrease the backbone rmsd between various homology models of calmodulin (CaM) and its crystal structure. Starting from a model of the Ca2+-saturated C-terminal domain of CaM, built from the structure of Ca2+-free recoverin on the basis of remote sequence homology, dipolar couplings are used to decrease the rmsd between the model and the crystal structure from 5.0 to 1.25 A. A better starting model, built from the crystal structure of Ca2+-saturated parvalbumin, decreases in rmsd from 1.25 to 0.93 A. Similarly, starting from the structure of the Ca2+-ligated CaM N-terminal domain, experimental dipolar couplings measured for the Ca2+-free form decrease the backbone rmsd relative to the refined solution structure of apo-CaM from 4.2 to 1.0 A.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1F71 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F71 OCA].
</div>
<div class="pdbe-citations 1f71" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings., Chou JJ, Li S, Bax A, J Biomol NMR. 2000 Nov;18(3):217-27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11142512 11142512]
*[[Calmodulin 3D structures|Calmodulin 3D structures]]
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
[[Category: Bax, A.]]
[[Category: Bax A]]
[[Category: Chou, J.]]
[[Category: Chou J]]
[[Category: Li, S.]]
[[Category: Li S]]
[[Category: Calcium binding]]
[[Category: Ef hand]]
[[Category: Four-helix bundle]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:58:53 2008''

Latest revision as of 08:28, 22 May 2024

REFINED SOLUTION STRUCTURE OF CALMODULIN C-TERMINAL DOMAIN

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