We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Structural Studies on Phospholamban and Implications for Regulation of the Ca<sup>2+</sup>-ATPase.
- Authors
MORTISHIRE-SMITH, RUSSELL J.; BROUGHTON, HOWARD; GARSKY, VICTOR M.; MAYER, ERNEST J.; JOHNSON, ROBERT G.
- Abstract
ABSTRACT: The cardiac sarcoplasmic reticulum (SR) protein phospholamban (PLB) is an endogenous inhibitor of the SR Ca2+-ATPase. Phosphorylation of PLB relieves this inhibition and up-regulates calcium transport. PLB has proved remarkably difficult to study by conventional solution-state nuclear magnetic resonance (NMR) methods, due primarily to the extreme hydrophobic nature of the protein and its propensity to form pentamers. That the C-terminal domain of PLB is helical and membrane spanning is now well established; the structure of the cytoplasmic domain is relatively ill defined. In order to discern the effect of phosphorylation on the structure of the cytoplasmic domain, we have characterized a variety of model peptides in several structure-inducing and/or lipid-mimicking environments using circular dichroism and solution-state NMR. The resolution of peptide structures obtained in aqueous trifluoroethanol was markedly improved by the incorporation of 15 N labels into the peptide backbone, allowing a variety of isotope edited, filtered, and resolved techniques to be applied. Molecular dynamics simulations on the full-length protein were combined with an analysis of published data to suggest a revised model for the structure of PLB.
- Publication
Annals of the New York Academy of Sciences, 1998, Vol 853, Issue 1, p63
- ISSN
0077-8923
- Publication type
Article
- DOI
10.1111/j.1749-6632.1998.tb08257.x