2lgf

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[[Image:2lgf.jpg|left|200px]]
 
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==Solution structure of Ca2+/calmodulin complexed with a peptide representing the calmodulin-binding domain of L-selectin==
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The line below this paragraph, containing "STRUCTURE_2lgf", creates the "Structure Box" on the page.
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<StructureSection load='2lgf' size='340' side='right'caption='[[2lgf]]' 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'>[[2lgf]] is a 2 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=2LGF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LGF 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_2lgf| PDB=2lgf | 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=2lgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lgf OCA], [https://pdbe.org/2lgf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lgf RCSB], [https://www.ebi.ac.uk/pdbsum/2lgf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lgf 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The L-selectin glycoprotein receptor mediates the initial steps of leukocyte migration into secondary lymphoid organs and sites of inflammation. Following cell activation through the engagement of G-protein-coupled receptors or immunoreceptors, the extracellular domains of L-selectin are rapidly shed, a process negatively controlled via the binding of the ubiquitous eukaryotic calcium-binding protein calmodulin to the cytoplasmic tail of L-selectin. Here we present the solution structure of calcium-calmodulin bound to a peptide encompassing the cytoplasmic tail and part of the transmembrane domain of L-selectin. The structure and accompanying biophysical study highlight the importance of both calcium and the transmembrane segment of L-selectin in the interaction between these two proteins, suggesting that by binding this region, calmodulin regulates in an "inside-out" fashion the ectodomain shedding of the receptor. Our structure provides the first molecular insight into the emerging new role for calmodulin as a transmembrane signaling partner.
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===Solution structure of Ca2+/calmodulin complexed with a peptide representing the calmodulin-binding domain of L-selectin===
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Structural Insights into Calmodulin-regulated L-selectin Ectodomain Shedding.,Gifford JL, Ishida H, Vogel HJ J Biol Chem. 2012 Aug 3;287(32):26513-27. Epub 2012 Jun 18. PMID:22711531<ref>PMID:22711531</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 2lgf" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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[[2lgf]] is a 2 chain structure with 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=2LGF OCA].
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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*[[Selectin|Selectin]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Gifford, J L.]]
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[[Category: Large Structures]]
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[[Category: Ishida, H.]]
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[[Category: Gifford JL]]
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[[Category: Vogel, H J.]]
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[[Category: Ishida H]]
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[[Category: Metal binding protein]]
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[[Category: Vogel HJ]]

Current revision

Solution structure of Ca2+/calmodulin complexed with a peptide representing the calmodulin-binding domain of L-selectin

PDB ID 2lgf

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