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1dmo

From Proteopedia

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{{Seed}}
 
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[[Image:1dmo.png|left|200px]]
 
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==CALMODULIN, NMR, 30 STRUCTURES==
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The line below this paragraph, containing "STRUCTURE_1dmo", creates the "Structure Box" on the page.
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<StructureSection load='1dmo' size='340' side='right'caption='[[1dmo]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1dmo]] 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=1DMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DMO FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dmo OCA], [https://pdbe.org/1dmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dmo RCSB], [https://www.ebi.ac.uk/pdbsum/1dmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dmo ProSAT]</span></td></tr>
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{{STRUCTURE_1dmo| PDB=1dmo | SCENE= }}
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dm/1dmo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1dmo ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The solution structure of Ca(2+)-free calmodulin has been determined by NMR spectroscopy, and is compared to the previously reported structure of the Ca(2+)-saturated form. The removal of Ca2+ causes the interhelical angles of four EF-hand motifs to increase by 36 degrees-44 degrees. This leads to major changes in surface properties, including the closure of the deep hydrophobic cavity essential for target protein recognition. Concerted movements of helices A and D with respect to B and C, and of helices E and H with respect to F and G are likely responsible for the cooperative Ca(2+)-binding property observed between two adjacent EF-hand sites in the amino- and carboxy-terminal domains.
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===CALMODULIN, NMR, 30 STRUCTURES===
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Calcium-induced conformational transition revealed by the solution structure of apo calmodulin.,Zhang M, Tanaka T, Ikura M Nat Struct Biol. 1995 Sep;2(9):758-67. PMID:7552747<ref>PMID:7552747</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1dmo" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_7552747}}, adds the Publication Abstract to the page
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 7552747 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_7552747}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1DMO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DMO OCA].
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==Reference==
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Calcium-induced conformational transition revealed by the solution structure of apo calmodulin., Zhang M, Tanaka T, Ikura M, Nat Struct Biol. 1995 Sep;2(9):758-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7552747 7552747]
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[[Category: Single protein]]
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[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Ikura, M.]]
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[[Category: Ikura M]]
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[[Category: Tanaka, T.]]
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[[Category: Tanaka T]]
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[[Category: Zhang, M.]]
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[[Category: Zhang M]]
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[[Category: Calcium-binding protein]]
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[[Category: Calcium-induced conformational change]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:18:22 2008''
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Current revision

CALMODULIN, NMR, 30 STRUCTURES

PDB ID 1dmo

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