Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/23318
Title: Structural basis for Ca2+ regulation in the Na+/Ca2+ exchanger.
Authors: Hilge, M
Aelen, J
Perrakis, A
Vuister, GW
First Published: Mar-2007
Citation: ANN N Y ACAD SCI, 2007, 1099, pp. 7-15
Abstract: Binding of Na+ and Ca2+ ions to the large cytosolic loop of the Na+/Ca2+ exchanger (NCX) regulates its ion transport across the plasma membrane. We determined the solution structures of two Ca2+-binding domains (CBD1 and CBD2) that, together with an alpha-catenin-like domain (CLD) form the regulatory exchanger loop. CBD1 and CBD2 constitute a novel Ca2+-binding motif and are very similar in the Ca2+-bound state. Strikingly, in the absence of Ca2+ the upper half of CBD1 unfolds while CBD2 maintains its structural integrity. Together with a sevenfold higher affinity for Ca2+ this suggests that CBD1 is the primary Ca2+ sensor. Specific point mutations in either domain largely allow the interchange of their functionality and uncover the mechanism underlying Ca2+ sensing in NCX.
DOI Link: 10.1196/annals.1387.030
ISSN: 0077-8923
Links: http://hdl.handle.net/2381/23318
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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