| pubmed-article:17996192 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17996192 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
| pubmed-article:17996192 | lifeskim:mentions | umls-concept:C2752508 | lld:lifeskim |
| pubmed-article:17996192 | lifeskim:mentions | umls-concept:C0205147 | lld:lifeskim |
| pubmed-article:17996192 | lifeskim:mentions | umls-concept:C1622525 | lld:lifeskim |
| pubmed-article:17996192 | lifeskim:mentions | umls-concept:C0070876 | lld:lifeskim |
| pubmed-article:17996192 | lifeskim:mentions | umls-concept:C1167322 | lld:lifeskim |
| pubmed-article:17996192 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17996192 | lifeskim:mentions | umls-concept:C0443288 | lld:lifeskim |
| pubmed-article:17996192 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:17996192 | pubmed:dateCreated | 2007-12-17 | lld:pubmed |
| pubmed-article:17996192 | pubmed:abstractText | The Ca2+-ATPase of cardiac muscle cells transports Ca2+ ions against a concentration gradient into the sarcoplasmic reticulum and is regulated by phospholamban, a 52-residue integral membrane protein. It is known that phospholamban inhibits the Ca2+ pump during muscle contraction and that inhibition is removed by phosphorylation of the protein during muscle relaxation. Phospholamban forms a pentameric complex with a central pore. The solid-state magic angle spinning (MAS) NMR measurements presented here address the structure of the phospholamban pentamer in the region of Gln22-Gln29. Rotational echo double resonance (REDOR) NMR measurements show that the side chain amide groups of Gln29 are in close proximity, consistent with a hydrogen-bonded network within the central pore. 13C MAS NMR measurements are also presented on phospholamban that is 1-13C-labeled at Leu52, the last residue of the protein. pH titration of the C-terminal carboxyl group suggests that it forms a ring of negative charge on the lumenal side of the sarcoplasmic reticulum membrane. The structural constraints on the phospholamban pentamer described in this study are discussed in the context of a multifaceted mechanism for Ca2+ regulation that may involve phospholamban as both an inhibitor of the Ca2+ ATPase and as an ion channel. | lld:pubmed |
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| pubmed-article:17996192 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17996192 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17996192 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17996192 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17996192 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17996192 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:17996192 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:17996192 | pubmed:author | pubmed-author:TomP APA | lld:pubmed |
| pubmed-article:17996192 | pubmed:author | pubmed-author:SmithSteven... | lld:pubmed |
| pubmed-article:17996192 | pubmed:author | pubmed-author:KawakamiToruT | lld:pubmed |
| pubmed-article:17996192 | pubmed:author | pubmed-author:FeiJeffrey... | lld:pubmed |
| pubmed-article:17996192 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17996192 | pubmed:volume | 1768 | lld:pubmed |
| pubmed-article:17996192 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17996192 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17996192 | pubmed:pagination | 2971-8 | lld:pubmed |
| pubmed-article:17996192 | pubmed:dateRevised | 2011-8-1 | lld:pubmed |
| pubmed-article:17996192 | pubmed:meshHeading | pubmed-meshheading:17996192... | lld:pubmed |
| pubmed-article:17996192 | pubmed:meshHeading | pubmed-meshheading:17996192... | lld:pubmed |
| pubmed-article:17996192 | pubmed:meshHeading | pubmed-meshheading:17996192... | lld:pubmed |
| pubmed-article:17996192 | pubmed:meshHeading | pubmed-meshheading:17996192... | lld:pubmed |
| pubmed-article:17996192 | pubmed:meshHeading | pubmed-meshheading:17996192... | lld:pubmed |
| pubmed-article:17996192 | pubmed:meshHeading | pubmed-meshheading:17996192... | lld:pubmed |
| pubmed-article:17996192 | pubmed:meshHeading | pubmed-meshheading:17996192... | lld:pubmed |
| pubmed-article:17996192 | pubmed:meshHeading | pubmed-meshheading:17996192... | lld:pubmed |
| pubmed-article:17996192 | pubmed:meshHeading | pubmed-meshheading:17996192... | lld:pubmed |
| pubmed-article:17996192 | pubmed:meshHeading | pubmed-meshheading:17996192... | lld:pubmed |
| pubmed-article:17996192 | pubmed:meshHeading | pubmed-meshheading:17996192... | lld:pubmed |
| pubmed-article:17996192 | pubmed:meshHeading | pubmed-meshheading:17996192... | lld:pubmed |
| pubmed-article:17996192 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17996192 | pubmed:articleTitle | Structural constraints on the transmembrane and juxtamembrane regions of the phospholamban pentamer in membrane bilayers: Gln29 and Leu52. | lld:pubmed |
| pubmed-article:17996192 | pubmed:affiliation | Department of Biochemistry and Cell Biology, Center for Structural Biology, Stony Brook University, Stony Brook, NY 11794-5115, USA. | lld:pubmed |
| pubmed-article:17996192 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17996192 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
