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      Defining the intramembrane binding mechanism of sarcolipin to calcium ATPase using solution NMR spectroscopy.

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          Abstract

          Sarcolipin (SLN) is an integral membrane protein that is expressed in both skeletal and cardiac muscle, where it inhibits SERCA (calcium ATPase) by lowering its apparent Ca2+ affinity in a manner similar to that of its homologue phospholamban (PLN). We use solution NMR to map the structural changes occurring within SLN upon interaction with the regulatory target, SERCA, co-reconstituting the two proteins in dodecylphosphocholine (DPC) detergent micelles, a system that preserves the native structure of SLN and the activity of SERCA, with the goal of comparing these interactions with those of the previously studied PLN-SERCA complex. Our analysis of the structural dynamics of SLN in DPC micelles shows this polypeptide to be partitioned into four subdomains: a short unstructured N terminus (residues 1-6), a short dynamic helix (residues 7-14), a more rigid helix (residues 15-26), and an unstructured C terminus (residues 27-31). Upon addition of SERCA, the different domains behave according to their dynamics, molding onto the surface of the enzyme. Remarkably, each domain of SLN behaves in a manner similar to that of the corresponding domains in PLN, supporting the hypothesis that both SLN and PLN bind SERCA in the same groove and with similar mechanisms.

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          Author and article information

          Journal
          J. Mol. Biol.
          Journal of molecular biology
          Elsevier BV
          0022-2836
          0022-2836
          Apr 28 2006
          : 358
          : 2
          Affiliations
          [1 ] Department of Chemistry, University of Minnesota, Minneapolis, MN 55455, USA.
          Article
          S0022-2836(06)00173-2
          10.1016/j.jmb.2006.02.005
          16519897
          73e837cd-4c71-4ec8-b5aa-db9ea4adf2bb
          History

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