2w73

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[[Image:2w73.png|left|200px]]
 
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==High-resolution structure of the complex between calmodulin and a peptide from calcineurin A==
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The line below this paragraph, containing "STRUCTURE_2w73", creates the "Structure Box" on the page.
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<StructureSection load='2w73' size='340' side='right'caption='[[2w73]], [[Resolution|resolution]] 1.45&Aring;' 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'>[[2w73]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W73 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W73 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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{{STRUCTURE_2w73| PDB=2w73 | SCENE= }}
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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=2w73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w73 OCA], [https://pdbe.org/2w73 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w73 RCSB], [https://www.ebi.ac.uk/pdbsum/2w73 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w73 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PP2BA_HUMAN PP2BA_HUMAN] Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1.<ref>PMID:15671020</ref> <ref>PMID:18838687</ref>
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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/w7/2w73_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=2w73 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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BACKGROUND: Calmodulin (CaM) is a ubiquitously expressed calcium sensor that engages in regulatory interactions with a large number of cellular proteins. Previously, a unique mode of CaM target recognition has been observed in the crystal structure of a complex between CaM and the CaM-binding domain of calcineurin A. METHODOLOGY/PRINCIPAL FINDINGS: We have solved a high-resolution crystal structure of a complex between CaM and the CaM-binding domain of calcineurin A in a novel crystal form, which shows a dimeric assembly of calmodulin, as observed before in the crystal state. We note that the conformation of CaM in this complex is very similar to that of unliganded CaM, and a detailed analysis revels that the CaM-binding motif in calcineurin A is of a novel '1-11' type. However, using small-angle X-ray scattering (SAXS), we show that the complex is fully monomeric in solution, and a structure of a canonically collapsed CaM-peptide complex can easily be fitted into the SAXS data. This result is also supported by size exclusion chromatography, where the addition of the ligand peptide decreases the apparent size of CaM. In addition, we studied the energetics of binding by isothermal titration calorimetry and found them to closely resemble those observed previously for ligand peptides from CaM-dependent kinases. CONCLUSIONS/SIGNIFICANCE: Our results implicate that CaM can also form a complex with the CaM-binding domain of calcineurin in a 1 ratio 1 stoichiometry, in addition to the previously observed 2 ratio 2 arrangement in the crystal state. At the structural level, going from 2 ratio 2 association to two 1 ratio 1 complexes will require domain swapping in CaM, accompanied by the characteristic bending of the central linker helix between the two lobes of CaM.
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===HIGH-RESOLUTION STRUCTURE OF THE COMPLEX BETWEEN CALMODULIN AND A PEPTIDE FROM CALCINEURIN A===
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Domain swapping and different oligomeric States for the complex between calmodulin and the calmodulin-binding domain of calcineurin a.,Majava V, Kursula P PLoS ONE. 2009;4(4):e5402. Epub 2009 Apr 30. PMID:19404396<ref>PMID:19404396</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 class="pdbe-citations 2w73" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19404396 is the PubMed ID number.
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{{ABSTRACT_PUBMED_19404396}}
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==About this Structure==
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[[2w73]] is a 8 chain structure of [[Calmodulin]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W73 OCA].
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==See Also==
==See Also==
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*[[Calmodulin]]
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:19404396</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Phosphoprotein phosphatase]]
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[[Category: Large Structures]]
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[[Category: Kursula, P.]]
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[[Category: Kursula P]]
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[[Category: Majava, V.]]
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[[Category: Majava V]]
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[[Category: Acetylation]]
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[[Category: Alternative splicing]]
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[[Category: Calcium]]
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[[Category: Calmodulin]]
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[[Category: Calmodulin-binding]]
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[[Category: Dimer]]
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[[Category: Ef hand]]
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[[Category: Hydrolase]]
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[[Category: Iron]]
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[[Category: Metal-binding]]
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[[Category: Metal-binding protein]]
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[[Category: Methylation]]
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[[Category: Nucleus]]
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[[Category: Peptide]]
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[[Category: Phosphoprotein]]
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[[Category: Polymorphism]]
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[[Category: Protein phosphatase]]
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[[Category: Ubl conjugation]]
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[[Category: Zinc]]
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Current revision

High-resolution structure of the complex between calmodulin and a peptide from calcineurin A

PDB ID 2w73

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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