This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1cmg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1cmg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cmg" /> '''NMR SOLUTION STRUCTURE OF CALCIUM-LOADED CAL...)
Current revision (08:21, 22 May 2024) (edit) (undo)
 
(19 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1cmg.gif|left|200px]]<br /><applet load="1cmg" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1cmg" />
 
-
'''NMR SOLUTION STRUCTURE OF CALCIUM-LOADED CALMODULIN CARBOXY-TERMINAL DOMAIN'''<br />
 
-
==Overview==
+
==NMR SOLUTION STRUCTURE OF CALCIUM-LOADED CALMODULIN CARBOXY-TERMINAL DOMAIN==
-
We have determined the solution structures of the apo and (Ca2+)2 forms of, the carboxy-terminal domain of calmodulin using multidimensional, heteronuclear nuclear magnetic resonance spectroscopy. The results show, that both forms adopt well-defined structures with essentially equal, secondary structure. A comparison of the structures of the two forms shows, that Ca2+ binding causes major rearrangements of the secondary structure, elements with changes in inter-residue distances of up to 15 A and, exposure of the hydrophobic interior of the four-helix bundle. Comparisons, with previously determined high-resolution X-ray structures and models of, calmodulin indicate that this domain is structurally autonomous.
+
<StructureSection load='1cmg' size='340' side='right'caption='[[1cmg]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1cmg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CMG FirstGlance]. <br>
 +
</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=1cmg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cmg OCA], [https://pdbe.org/1cmg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cmg RCSB], [https://www.ebi.ac.uk/pdbsum/1cmg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cmg ProSAT]</span></td></tr>
 +
</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 ==
 +
[[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/cm/1cmg_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1cmg ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
We have determined the solution structures of the apo and (Ca2+)2 forms of the carboxy-terminal domain of calmodulin using multidimensional heteronuclear nuclear magnetic resonance spectroscopy. The results show that both forms adopt well-defined structures with essentially equal secondary structure. A comparison of the structures of the two forms shows that Ca2+ binding causes major rearrangements of the secondary structure elements with changes in inter-residue distances of up to 15 A and exposure of the hydrophobic interior of the four-helix bundle. Comparisons with previously determined high-resolution X-ray structures and models of calmodulin indicate that this domain is structurally autonomous.
-
==About this Structure==
+
Calcium-induced structural changes and domain autonomy in calmodulin.,Finn BE, Evenas J, Drakenberg T, Waltho JP, Thulin E, Forsen S Nat Struct Biol. 1995 Sep;2(9):777-83. PMID:7552749<ref>PMID:7552749</ref>
-
1CMG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CMG OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Calcium-induced structural changes and domain autonomy in calmodulin., Finn BE, Evenas J, Drakenberg T, Waltho JP, Thulin E, Forsen S, Nat Struct Biol. 1995 Sep;2(9):777-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7552749 7552749]
+
</div>
-
[[Category: Bos taurus]]
+
<div class="pdbe-citations 1cmg" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Drakenberg, T.]]
+
-
[[Category: Evenas, J.]]
+
-
[[Category: Finn, B.E.]]
+
-
[[Category: Forsen, S.]]
+
-
[[Category: Thulin, E.]]
+
-
[[Category: Waltho, J.P.]]
+
-
[[Category: calcium-binding protein]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:34:53 2007''
+
==See Also==
 +
*[[Calmodulin 3D structures|Calmodulin 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Bos taurus]]
 +
[[Category: Large Structures]]
 +
[[Category: Drakenberg T]]
 +
[[Category: Evenas J]]
 +
[[Category: Finn BE]]
 +
[[Category: Forsen S]]
 +
[[Category: Thulin E]]
 +
[[Category: Waltho JP]]

Current revision

NMR SOLUTION STRUCTURE OF CALCIUM-LOADED CALMODULIN CARBOXY-TERMINAL DOMAIN

PDB ID 1cmg

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cmg"
Personal tools