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Structural perspectives of phospholamban, a helical transmembrane pentamer.

Phospholamban is a 52-amino-acid protein that assembles into a pentamer in sarcoplasmic reticulum membranes. The protein has a role in the regulation of the resident calcium ATPase through an inhibitory association that can be reversed by phosphorylation. The phosphorylation of phospholamban is initiated by beta-adrenergic stimulation, identifying phospholamban as an important component in the stimulation of cardiac activity by beta-agonists. In this role of phospholamban that has motivated studies in recent decades. There is evidence that phospholamban may also function as a Ca(2+)-selective ion channel. The structural properties of phospholamban have been studied by mutagenesis, modeling, and spectroscopy, resulting in a new view of the organization of this key molecule in membranes.[1]

References

  1. Structural perspectives of phospholamban, a helical transmembrane pentamer. Arkin, I.T., Adams, P.D., Brünger, A.T., Smith, S.O., Engelman, D.M. Annual review of biophysics and biomolecular structure. (1997) [Pubmed]
 
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