1dmo
From Proteopedia
(Difference between revisions)
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==CALMODULIN, NMR, 30 STRUCTURES== | ==CALMODULIN, NMR, 30 STRUCTURES== | ||
| - | <StructureSection load='1dmo' size='340' side='right'caption='[[1dmo | + | <StructureSection load='1dmo' size='340' side='right'caption='[[1dmo]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1dmo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=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> | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [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. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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]. | </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]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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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| - | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1dmo" 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: African clawed frog]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Xenopus laevis]] |
| - | [[Category: | + | [[Category: Ikura M]] |
| - | + | [[Category: Tanaka T]] | |
| - | [[Category: | + | [[Category: Zhang M]] |
| - | [[Category: | + | |
Revision as of 09:51, 20 March 2024
CALMODULIN, NMR, 30 STRUCTURES
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