ArticleJournal of molecular biology2008
Structure and dynamics of Ca2+-binding domain 1 of the Na+/Ca2+ exchanger in the presence and in the absence of Ca2+.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- CALX-CBD1 CaBiophysical journal · 2020Article
- Modulation of the cardiac NaCell calcium · 2020Review
- Functional protein dynamics on uncharted time scales detected by nanoparticle-assisted NMR spin relaxation.Science advances · 2019Article
- Reliable resonance assignments of selected residues of proteins with known structure based on empirical NMR chemical shift prediction.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- Structural arrangement of the intracellular Ca2+ binding domains of the cardiac Na+/Ca2+ exchanger (NCX1.1): effects of Ca2+ binding.The Journal of biological chemistry · 2013Article
- Structural basis of the Ca2+ inhibitory mechanism of Drosophila Na+/Ca2+ exchanger CALX and its modification by alternative splicing.Structure (London, England : 1993) · 2011Article
- Ca2+ binding alters the interdomain flexibility between the two cytoplasmic calcium-binding domains in the Na+/Ca2+ exchanger.The Journal of biological chemistry · 2011Article
- Proton-sensing Ca2+ binding domains regulate the cardiac Na+/Ca2+ exchanger.The Journal of biological chemistry · 2011Article
- Ca2+-dependent structural rearrangements within Na+-Ca2+ exchanger dimers.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Essential role of the CBD1-CBD2 linker in slow dissociation of Ca2+ from the regulatory two-domain tandem of NCX1.The Journal of biological chemistry · 2010Article
- Crystal structures of progressive Ca2+ binding states of the Ca2+ sensor Ca2+ binding domain 1 (CBD1) from the CALX Na+/Ca2+ exchanger reveal incremental conformational transitions.The Journal of biological chemistry · 2010Article
- Roles of two Ca2+-binding domains in regulation of the cardiac Na+-Ca2+ exchanger.The Journal of biological chemistry · 2009Article
- Structure and functional analysis of a Ca2+ sensor mutant of the Na+/Ca2+ exchanger.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The Na(+)/Ca(2+) exchanger is the major exporter of Ca(2+) across the cell membrane of cardiomyocytes. The activity of the exchanger is regulated by a large intracellular loop that contains two Ca(2+)-binding domains, calcium-binding domain (CBD) 1 and CBD2. CBD1 binds Ca(2+) with much higher affinity than CBD2 and is considered to be the primary Ca(2+) sensor. The effect of Ca(2+) 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 Ca(2+) 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, Ca(2+) binding restricts the mobility of the major acidic segment and affects the dynamics of several nearby binding loops. These observations indicate that Ca(2+) elicits a local transition to a well-ordered coordination geometry in the CBD1-binding site.
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