1jdm: Difference between revisions
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[[ | ==NMR Structure of Sarcolipin== | ||
<StructureSection load='1jdm' size='340' side='right' caption='[[1jdm]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1jdm]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JDM FirstGlance]. <br> | |||
</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=1jdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jdm RCSB], [http://www.ebi.ac.uk/pdbsum/1jdm PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Sarcolipin (SLN) is a 31 amino acid integral membrane protein that regulates Ca-ATPase activity in skeletal muscle. Here, we report the three-dimensional structure and topology of synthetic SLN in lipid environments, as determined by solution and solid-state NMR spectroscopy. 2D solution NMR experiments were performed on SLN solubilized in sodium dodecyl sulfate (SDS) micelles. We found that SLN adopts a highly defined alpha-helical conformation from F9 through R27, with a backbone RMSD of 0.65 A and a side chain RMSD of 1.66 A. The N-terminus (M1 through L8) and the C-terminus (S28 through Y31) are mostly unstructured. The orientation of the SLN was determined using one-dimensional (15)N NMR solid-state spectroscopy. The protein was incorporated into phospholipid bilayers prepared from a mixture of 1,2-dioleoyl-sn-glycero-3-phosphocholine and 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine. The (15)N chemical shift solid-state spectra from selectively labeled SLN samples indicate that SLN orients perpendicularly to the plane of the membrane bilayers. These results support the proposed mechanism of Ca-ATPase regulation of SLN via protein-protein intramembranous interactions between the highly conserved transmembrane domains of the Ca-ATPase and the conserved transmembrane domain of SLN. | |||
Structure and orientation of sarcolipin in lipid environments.,Mascioni A, Karim C, Barany G, Thomas DD, Veglia G Biochemistry. 2002 Jan 15;41(2):475-82. PMID:11781085<ref>PMID:11781085</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Mascioni, A.]] | [[Category: Mascioni, A.]] | ||
[[Category: Veglia, G.]] | [[Category: Veglia, G.]] | ||
[[Category: Helix]] | [[Category: Helix]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
Revision as of 05:40, 8 June 2014
NMR Structure of Sarcolipin
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