View source for 2lpf


==R state structure of monomeric phospholamban (C36A, C41F, C46A)==
<StructureSection load='2lpf' size='340' side='right'caption='[[2lpf]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lpf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LPF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LPF 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lpf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lpf OCA], [https://pdbe.org/2lpf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lpf RCSB], [https://www.ebi.ac.uk/pdbsum/2lpf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lpf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PPLA_RABIT PPLA_RABIT] Phospholamban has been postulated to regulate the activity of the calcium pump of cardiac sarcoplasmic reticulum.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Phospholamban is an integral membrane protein that controls the calcium balance in cardiac muscle cells. As the function and regulation of this protein require the active involvement of low populated states in equilibrium with the native state, it is of great interest to acquire structural information about them. In this work we determine the conformations and populations of the ground state and the three main excited states of phospholamban by incorporating nuclear magnetic resonance (NMR) residual dipolar couplings (RDCs) as replica-averaged structural restraints in molecular dynamics simulations. We then provide a description of the manner in which phosphorylation at Ser16 modulates the activity of the protein by increasing the populations of its excited states. These results demonstrate that approach that we describe provides a detailed characterisation of the different states of phospholamban that determine the function and regulation of this membrane protein. We anticipate that the availability of conformational ensembles will provide opportunities for the development of therapeutic strategies to control the activity of phospholamban by modulating the relative populations of its conformational substates.

Structures of the Excited States of Phospholamban and Shifts in their Populations upon Phosphorylation.,De Simone A, Gustavsson MB, Montalvao RW, Shi L, Veglia G, Vendruscolo M Biochemistry. 2013 Aug 22. PMID:23968132<ref>PMID:23968132</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lpf" style="background-color:#fffaf0;"></div>

==See Also==
*[[Phospholamban|Phospholamban]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: De Simone A]]
[[Category: Gustavsson M]]
[[Category: Montalvao RW]]
[[Category: Shi L]]
[[Category: Veglia G]]
[[Category: Vendruscolo M]]