2hf5

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{{Seed}}
 
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[[Image:2hf5.png|left|200px]]
 
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==The structure and function of a novel two-site calcium-binding fragment of calmodulin==
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The line below this paragraph, containing "STRUCTURE_2hf5", creates the "Structure Box" on the page.
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<StructureSection load='2hf5' size='340' side='right'caption='[[2hf5]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2hf5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HF5 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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{{STRUCTURE_2hf5| PDB=2hf5 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hf5 OCA], [https://pdbe.org/2hf5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hf5 RCSB], [https://www.ebi.ac.uk/pdbsum/2hf5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hf5 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[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.
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hf/2hf5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2hf5 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Calmodulin (CaM) is an EF-hand protein composed of two calcium (Ca(2+))-binding EF-hand motifs in its N-domain (EF-1 and EF-2) and two in its C-domain (EF-3 and EF-4). In this study, we examined the structure, dynamics, and Ca(2+)-binding properties of a fragment of CaM containing only EF-2 and EF-3 and the intervening linker sequence (CaM2/3). Based on NMR spectroscopic analyses, Ca(2+)-free CaM2/3 is predominantly unfolded, but upon binding Ca(2+), adopts a monomeric structure composed of two EF-hand motifs bridged by a short antiparallel beta-sheet. Despite having an "even-odd" pairing of EF-hands, the tertiary structure of CaM2/3 is similar to both the "odd-even" paired N- and C-domains of Ca(2+)-ligated CaM, with the conformationally flexible linker sequence adopting the role of an inter-EF-hand loop. However, unlike either CaM domain, CaM2/3 exhibits stepwise Ca(2+) binding with a K (d1) = 30 +/- 5 microM to EF-3, and a K (d2) &gt; 1000 microM to EF-2. Binding of the first equivalent of Ca(2+) induces the cooperative folding of CaM2/3. In the case of native CaM, stacking interactions between four conserved aromatic residues help to hold the first and fourth helices of each EF-hand domain together, while the loop between EF-hands covalently tethers the second and third helices. In contrast, these aromatic residues lie along the second and third helices of CaM2/3, and thus are positioned adjacent to the loop between its "even-odd" paired EF-hands. This nonnative hydrophobic core packing may contribute to the weak Ca(2+) affinity exhibited by EF-2 in the context of CaM2/3.
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===The structure and function of a novel two-site calcium-binding fragment of calmodulin===
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Calcium-induced folding of a fragment of calmodulin composed of EF-hands 2 and 3.,Lakowski TM, Lee GM, Okon M, Reid RE, McIntosh LP Protein Sci. 2007 Jun;16(6):1119-32. Epub 2007 May 1. PMID:17473011<ref>PMID:17473011</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2hf5" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17473011}}, adds the Publication Abstract to the page
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17473011 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17473011}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2HF5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HF5 OCA].
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==Reference==
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Calcium-induced folding of a fragment of calmodulin composed of EF-hands 2 and 3., Lakowski TM, Lee GM, Okon M, Reid RE, McIntosh LP, Protein Sci. 2007 Jun;16(6):1119-32. Epub 2007 May 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17473011 17473011]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Lakowski, T M.]]
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[[Category: Lakowski TM]]
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[[Category: Lee, G M.]]
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[[Category: Lee GM]]
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[[Category: McIntosh, L P.]]
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[[Category: McIntosh LP]]
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[[Category: Reid, R E.]]
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[[Category: Reid RE]]
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[[Category: Calcium-binding]]
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[[Category: Calmodulin]]
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[[Category: Calmodulin fragment]]
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[[Category: Ef-hand]]
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[[Category: Hlh]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:35:24 2008''
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Current revision

The structure and function of a novel two-site calcium-binding fragment of calmodulin

PDB ID 2hf5

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