Structure and Dynamics of Ca2 +-Binding Domain 1 of the Na +/Ca2 + Exchanger in the Presence and in the Absence of Ca2 +

Eric Johnson, Lei Bruschweiler-Li, Scott A. Showalter, Geerten W. Vuister, Fengli Zhang, Rafael Brüschweiler

Research output: Contribution to journalArticlepeer-review

27 Scopus citations


The Na +/Ca2 + exchanger is the major exporter of Ca2 + across the cell membrane of cardiomyocytes. The activity of the exchanger is regulated by a large intracellular loop that contains two Ca2 +-binding domains, calcium-binding domain (CBD) 1 and CBD2. CBD1 binds Ca2 + with much higher affinity than CBD2 and is considered to be the primary Ca2 + sensor. The effect of Ca2 + on the structure and dynamics of CBD1 has been characterized by NMR spectroscopy using chemical shifts, residual dipolar couplings, and spin relaxation. Residual dipolar couplings are used in a new way for residue selection in the determination of the anisotropic rotational diffusion tensor from spin relaxation data. The results provide a highly consistent description across these complementary data sets and show that Ca2 + binding is accompanied by a selective conformational change among the binding site residues. Residues that exhibit a significant conformational change are also sites of altered dynamics. In particular, Ca2 + binding restricts the mobility of the major acidic segment and affects the dynamics of several nearby binding loops. These observations indicate that Ca2 + elicits a local transition to a well-ordered coordination geometry in the CBD1-binding site.

Original languageEnglish (US)
Pages (from-to)945-955
Number of pages11
JournalJournal of Molecular Biology
Issue number3
StatePublished - Mar 28 2008

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Molecular Biology


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