2ix7
From Proteopedia
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| - | {{STRUCTURE_2ix7| PDB=2ix7 | SCENE= }} | ||
| - | ===Structure of apo-calmodulin bound to unconventional myosin V=== | ||
| - | {{ABSTRACT_PUBMED_17151196}} | ||
| - | == | + | ==Structure of apo-calmodulin bound to unconventional myosin V== |
| - | [[http://www. | + | <StructureSection load='2ix7' size='340' side='right'caption='[[2ix7]], [[Resolution|resolution]] 2.50Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2ix7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IX7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IX7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2ix7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ix7 OCA], [https://pdbe.org/2ix7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ix7 RCSB], [https://www.ebi.ac.uk/pdbsum/2ix7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ix7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CALM1_MOUSE CALM1_MOUSE] Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2.[UniProtKB:P0DP23] | ||
| + | == 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/ix/2ix7_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2ix7 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A 2.5-A resolution structure of calcium-free calmodulin (CaM) bound to the first two IQ motifs of the murine myosin V heavy chain reveals an unusual CaM conformation. The C-terminal lobe of each CaM adopts a semi-open conformation that grips the first part of the IQ motif (IQxxxR), whereas the N-terminal lobe adopts a closed conformation that interacts more weakly with the second part of the motif (GxxxR). Variable residues in the IQ motif play a critical role in determining the precise structure of the bound CaM, such that even the consensus residues of different motifs show unique interactions with CaM. This complex serves as a model for the lever arm region of many classes of unconventional myosins, as well as other IQ motif-containing proteins such as neuromodulin and IQGAPs. | ||
| - | + | Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features.,Houdusse A, Gaucher JF, Krementsova E, Mui S, Trybus KM, Cohen C Proc Natl Acad Sci U S A. 2006 Dec 19;103(51):19326-31. Epub 2006 Dec 6. PMID:17151196<ref>PMID:17151196</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2ix7" style="background-color:#fffaf0;"></div> | |
| - | == | + | ==See Also== |
| - | + | *[[Calmodulin 3D structures|Calmodulin 3D structures]] | |
| - | [[ | + | *[[Myosin 3D Structures|Myosin 3D Structures]] |
| - | [[ | + | == References == |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
| - | [[Category: | + | [[Category: Mus musculus]] |
| - | [[Category: | + | [[Category: Cohen C]] |
| - | [[Category: | + | [[Category: Gaucher JF]] |
| - | [[Category: | + | [[Category: Houdusse A]] |
| - | [[Category: | + | [[Category: Krementsova E]] |
| - | [[Category: | + | [[Category: Mui S]] |
| - | [[Category: | + | [[Category: Trybus KM]] |
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Current revision
Structure of apo-calmodulin bound to unconventional myosin V
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Categories: Large Structures | Mus musculus | Cohen C | Gaucher JF | Houdusse A | Krementsova E | Mui S | Trybus KM
