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[[Image:2lgf.png|left|200px]]
==Solution structure of Ca2+/calmodulin complexed with a peptide representing the calmodulin-binding domain of L-selectin==
<StructureSection load='2lgf' size='340' side='right' caption='[[2lgf]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LGF FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene><br>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2, CAM3, CAMC, CAMIII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lgf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lgf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lgf RCSB], [http://www.ebi.ac.uk/pdbsum/2lgf PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


{{STRUCTURE_2lgf|  PDB=2lgf  |  SCENE=  }}
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>


===Solution structure of Ca2+/calmodulin complexed with a peptide representing the calmodulin-binding domain of L-selectin===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


{{ABSTRACT_PUBMED_22711531}}
==See Also==
 
*[[Calmodulin|Calmodulin]]
==About this Structure==
*[[Selectin|Selectin]]
[[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].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:022711531</ref><references group="xtra"/>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Gifford, J L.]]
[[Category: Gifford, J L.]]
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