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1deg
From Proteopedia
(Difference between revisions)
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<StructureSection load='1deg' size='340' side='right'caption='[[1deg]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='1deg' size='340' side='right'caption='[[1deg]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1deg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1deg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DEG FirstGlance]. <br> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| + | <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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1deg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1deg OCA], [https://pdbe.org/1deg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1deg RCSB], [https://www.ebi.ac.uk/pdbsum/1deg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1deg ProSAT]</span></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=1deg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1deg OCA], [https://pdbe.org/1deg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1deg RCSB], [https://www.ebi.ac.uk/pdbsum/1deg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1deg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CALM_BOVIN CALM_BOVIN] 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. Together with CEP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (By similarity). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 17: | Line 20: | ||
</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=1deg ConSurf]. | </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=1deg ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The crystal structure of a mutant calmodulin (CaM) lacking Glu-84 has been refined to R = 0.23 using data measured to 2.9-A resolution. In native CaM the central helix is fully extended, and the molecule is dumbbell shaped. In contrast, the deletion of Glu-84 causes a bend of 95 degrees in the linker region of the central helix at Ile-85. However, EF-hand domains 1 and 2 (lobe 1,2) do not touch lobe 3,4. The length, by alpha-carbon separation, of des-Glu84-CaM is 56 A; that of native CaM is 64 A. The shape of des-Glu84-CaM is similar to that of native CaM, as it is bound to the target peptide of myosin light-chain kinase. This result supports the proposal that the linker region of the central helix of CaM functions as a flexible tether. | ||
| - | |||
| - | The linker of des-Glu84-calmodulin is bent.,Raghunathan S, Chandross RJ, Cheng BP, Persechini A, Sobottka SE, Kretsinger RH Proc Natl Acad Sci U S A. 1993 Jul 15;90(14):6869-73. PMID:8341712<ref>PMID:8341712</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1deg" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Calmodulin 3D structures|Calmodulin 3D structures]] | *[[Calmodulin 3D structures|Calmodulin 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bos taurus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Chandross | + | [[Category: Chandross R]] |
| - | [[Category: Cheng | + | [[Category: Cheng BP]] |
| - | [[Category: Kretsinger | + | [[Category: Kretsinger RH]] |
| - | [[Category: Persechini | + | [[Category: Persechini A]] |
| - | [[Category: Raghunathan | + | [[Category: Raghunathan S]] |
| - | [[Category: Sobottk | + | [[Category: Sobottk SE]] |
| - | + | ||
Current revision
THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURE
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