1cll: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1cll.gif|left|200px]]<br />
-<applet load="1cll" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1cll, resolution 1.7&Aring;" />
-'''CALMODULIN STRUCTURE REFINED AT 1.7 ANGSTROMS RESOLUTION'''<br />
-==Overview==
+==CALMODULIN STRUCTURE REFINED AT 1.7 ANGSTROMS RESOLUTION==
-We have determined and refined the crystal structure of a recombinant, calmodulin at 1.7 A resolution. The structure was determined by molecular, replacement, using the 2.2 A published native bovine brain structure as, the starting model. The final crystallographic R-factor, using 14,469, reflections in the 10.0 to 1.7 A range with structure factors exceeding, 0.5 sigma, is 0.216. Bond lengths and bond angle distances have, root-mean-square deviations from ideal values of 0.009 A and 0.032 A, respectively. The final model consists of 1279 non-hydrogen atoms, including four calcium ions, 1130 protein atoms, including three Asp118, side-chain atoms in double conformation, 139 water molecules and one, ethanol molecule. The electron densities for residues 1 to 4 and 148 of, calmodulin are poorly defined, and not included in our model, except for, main-chain atoms of residue 4. The calmodulin structure from our crystals, is very similar to the earlier 2.2 A structure described by Babu and, coworkers with a root-mean-square deviation of 0.36 A. Calmodulin remains, a dumb-bell-shaped molecule, with similar lobes and connected by a central, alpha-helix. Each lobe contains three alpha-helices and two Ca2+ binding, EF hand loops, with a short antiparallel beta-sheet between adjacent EF, hand loops and one non-EF hand loop. There are some differences in the, structure of the central helix. The crystal packing is extensively, studied, and facile crystal growth along the z-axis of the triclinic, crystals is explained. Herein, we describe hydrogen bonding in the various, secondary structure elements and hydration of calmodulin.
+<StructureSection load='1cll' size='340' side='right'caption='[[1cll]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1cll]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The August 2003 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Calmodulin''  by Shuchismita Dutta and David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2003_8 10.2210/rcsb_pdb/mom_2003_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CLL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CLL 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]] 1.7&#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>, <scene name='pdbligand=EOH:ETHANOL'>EOH</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=1cll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cll OCA], [https://pdbe.org/1cll PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cll RCSB], [https://www.ebi.ac.uk/pdbsum/1cll PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cll ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of CPVT4.  The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of LQT14.
+== Function ==
+[https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (PubMed:16760425). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696).<ref>PMID:16760425</ref> <ref>PMID:23893133</ref> <ref>PMID:26969752</ref> <ref>PMID:27165696</ref>
+== 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/cl/1cll_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=1cll 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|Calmodulin]]
+*[[Calmodulin 3D structures|Calmodulin 3D structures]]
-==About this Structure==
+== References ==
-CLL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and EOH as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1CLL with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb44_1.html Calmodulin]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CLL OCA].
+<references/>
+__TOC__
-==Reference==
+</StructureSection>
-Calmodulin structure refined at 1.7 A resolution., Chattopadhyaya R, Meador WE, Means AR, Quiocho FA, J Mol Biol. 1992 Dec 20;228(4):1177-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1474585 1474585]
 [[Category: Calmodulin]]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Chattopadhyaya, R.]]
+[[Category: RCSB PDB Molecule of the Month]]
-[[Category: Quiocho, F.A.]]
+[[Category: Chattopadhyaya R]]
-[[Category: CA]]
+[[Category: Quiocho FA]]
-[[Category: EOH]]
-[[Category: calcium-binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:23:02 2007''