1deg: Difference between revisions

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OCA

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-[[Image:1deg.gif|left|200px]]<br />
-<applet load="1deg" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1deg, resolution 2.9&Aring;" />
-'''THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURE'''<br />
-==Overview==
+==THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURE==
-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.
+<StructureSection load='1deg' size='340' side='right'caption='[[1deg]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</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>
+</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/de/1deg_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=1deg ConSurf].
+<div style="clear:both"></div>
-==Disease==
+==See Also==
-Known diseases associated with this structure: Cavernous malformations of CNS and retina OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604214 604214]], Cerebral cavernous malformations-1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604214 604214]], Hyperkeratotic cutaneous capillary-venous malformations associated with cerebral capillary malformations OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604214 604214]], Leukemia, acute T-cell lymphoblastic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603025 603025]], Leukemia, acute myeloid OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603025 603025]]
+*[[Calmodulin 3D structures|Calmodulin 3D structures]]
+__TOC__
-==About this Structure==
+</StructureSection>
-DEG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DEG OCA].
-==Reference==
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8341712 8341712]
 [[Category: Bos taurus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Chandross, R.]]
+[[Category: Chandross R]]
-[[Category: Cheng, B.P.]]
+[[Category: Cheng BP]]
-[[Category: Kretsinger, R.H.]]
+[[Category: Kretsinger RH]]
-[[Category: Persechini, A.]]
+[[Category: Persechini A]]
-[[Category: Raghunathan, S.]]
+[[Category: Raghunathan S]]
-[[Category: Sobottk, S.E.]]
+[[Category: Sobottk SE]]
-[[Category: CA]]
-[[Category: calcium-binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:31:30 2007''