4hex
From Proteopedia
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| - | [[ | + | ==A novel conformation of calmodulin== |
| + | <StructureSection load='4hex' size='340' side='right' caption='[[4hex]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4hex]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HEX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HEX FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hex OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hex RCSB], [http://www.ebi.ac.uk/pdbsum/4hex PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Calmodulin (CaM) is a highly conserved eukaryotic protein that binds specifically to more than 100 target proteins in response to calcium (Ca(2+)) signal. CaM adopts a considerable degree of structural plasticity to accomplish this physiological role; however, the nature and extent of this plasticity remain to be fully understood. Here, we report the crystal structure of a novel trans conformation of ligand-free CaM where the relative disposition of two lobes of CaM is different, a conformation to-date not reported. While no major structural changes were observed in the independent N- and C-lobes as compared with previously reported structures of Ca(2+)/CaM, the central helix was tilted by approximately 90 degrees at Arg75. This is the first crystal structure of CaM to show a drastic conformational change in the central helix, and reveals one of several possible conformations of CaM to engage with its binding partner. | ||
| - | + | A novel trans conformation of ligand-free calmodulin.,Kumar V, Chichili VP, Tang X, Sivaraman J PLoS One. 2013;8(1):e54834. doi: 10.1371/journal.pone.0054834. Epub 2013 Jan 29. PMID:23382982<ref>PMID:23382982</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| - | + | ==See Also== | |
| - | + | *[[Calmodulin|Calmodulin]] | |
| - | == | + | == References == |
| - | [[ | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Chichili, V P.R | + | [[Category: Chichili, V P.R]] |
| - | [[Category: Kumar, V | + | [[Category: Kumar, V]] |
| - | [[Category: Sivaraman, J | + | [[Category: Sivaraman, J]] |
[[Category: Calcium binding]] | [[Category: Calcium binding]] | ||
[[Category: Calcium binding protein]] | [[Category: Calcium binding protein]] | ||
Revision as of 14:40, 25 December 2014
A novel conformation of calmodulin
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