View source for 2lcp


==NMR structure of calcium loaded, un-myristoylated human NCS-1==
<StructureSection load='2lcp' size='340' side='right'caption='[[2lcp]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lcp]] 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=2LCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LCP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lcp OCA], [https://pdbe.org/2lcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lcp RCSB], [https://www.ebi.ac.uk/pdbsum/2lcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lcp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NCS1_HUMAN NCS1_HUMAN] Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin (By similarity). Stimulates PI4KB kinase activity (By similarity). Involved in long-term synaptic plasticity through its interaction with PICK1 (By similarity). May also play a role in neuron differentiation through inhibition of the activity of N-type voltage-gated calcium channel (By similarity).
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== Publication Abstract from PubMed ==
Neuronal calcium sensor 1 (NCS-1) and orthologs are expressed in all organisms from yeast to humans. In the latter, NCS-1 plays an important role in neurotransmitter release and interacts with a plethora of binding partners mostly through a large solvent-exposed hydrophobic crevice. The structural basis behind the multispecific binding profile is not understood. To begin to address this, we applied NMR spectroscopy to determine the solution structure of calcium-bound human NCS-1. The structure in solution demonstrates interdomain flexibility and, in the absence of a binding partner, the C-terminal tail residues occupy the hydrophobic crevice as a ligand mimic. A variant with a C-terminal tail deletion shows lack of a defined structure but maintained cooperative unfolding and dramatically reduced global stability. The results suggest that the C-terminal tail is important for regulating the conformational stability of the Ca(2+)-activated state. Furthermore, a single amino acid mutation that was recently diagnosed in a patient with autistic spectrum disorder was seen to affect the C-terminal tail and binding crevice in NCS-1.

The C-Terminal Tail of Human Neuronal Calcium Sensor 1 Regulates the Conformational Stability of the Ca(2+)-Activated State.,Heidarsson PO, Bjerrum-Bohr IJ, Jensen GA, Pongs O, Finn BE, Poulsen FM, Kragelund BB J Mol Biol. 2011 Dec 29. PMID:22227393<ref>PMID:22227393</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lcp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bellucci L]]
[[Category: Bjerrum-Bohr IJ]]
[[Category: Corni S]]
[[Category: Di Felice R]]
[[Category: Finn BE]]
[[Category: Gitte J]]
[[Category: Heidarsson PO]]
[[Category: Kragelund B]]
[[Category: Poulsen FM]]