Structural highlights
Disease
[ATNG_HUMAN] Autosomal dominant primary hypomagnesemia with hypocalcuria. The disease is caused by mutations affecting the gene represented in this entry.
Function
[ATNG_HUMAN] May be involved in forming the receptor site for cardiac glycoside binding or may modulate the transport function of the sodium ATPase.
Publication Abstract from PubMed
FXYD2 is a membrane protein responsible for regulating the function of the Na,K-ATPase in mammalian kidney epithelial cells. Here we report the structure of FXYD2b, one of two splice variants of the protein, determined by NMR spectroscopy in detergent micelles. Solid-state NMR characterization of the protein embedded in phospholipid bilayers indicates that several arginine side chains may be involved in hydrogen bond interactions with the phospholipid polar head groups. The structure and the NMR data suggest that FXYD2b could regulate the Na,K-ATPase by modulating the effective membrane surface electrostatics near the ion binding sites of the pump. This article is part of a Special Issue entitled: NMR Spectroscopy for Atomistic Views of Biomembranes and Cell Surfaces.
Structure of the Na,K-ATPase regulatory protein FXYD2b in micelles: Implications for membrane-water interfacial arginines.,Gong XM, Ding Y, Yu J, Yao Y, Marassi FM Biochim Biophys Acta. 2014 May 2. pii: S0005-2736(14)00156-4. doi:, 10.1016/j.bbamem.2014.04.021. PMID:24794573[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gong XM, Ding Y, Yu J, Yao Y, Marassi FM. Structure of the Na,K-ATPase regulatory protein FXYD2b in micelles: Implications for membrane-water interfacial arginines. Biochim Biophys Acta. 2014 May 2. pii: S0005-2736(14)00156-4. doi:, 10.1016/j.bbamem.2014.04.021. PMID:24794573 doi:http://dx.doi.org/10.1016/j.bbamem.2014.04.021
