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- W2021125003 abstract "The Na+/H+ exchanger isoform 1 (NHE1) is an integral membrane protein important in the regulation of intracellular pH in the heart by exchanging one intracellular H+ for one extracellular Na+. It contains an N-terminal transmembrane (TM) domain responsible for ion transport and a C-terminal, cytoplasmic, regulatory domain. There is currently no high-resolution structure of NHE1; however, a topology model of the protein by Wakabayashi et al. (J. Biol. Chem.275, 7942) suggests that the membrane domain (amino acids 1-500) contains 12 TM helices. We have previously used NMR spectroscopy to determine the structures of peptides representing several TM helices from NHE1. Structures have been determined for TM IV in organic tri-solvent mixture, and for TM helices VII, IX, XI, and VI in DPC micelles. To provide further insight into the three-dimensional structure of NHE1, we are attempting to express and determine the structures of multiple TM helices. We have recently expressed and purified a two-TM helix segment representing TM VI-VII (amino acids 226-274) of NHE1. These two TM helices have been previously shown to be important in NHE1 function. Furthermore, modelling of NHE1 by Landau et al. (J. Biol. Chem. 282, 37854) suggest that these two helices interact and play key roles in ion transport. We are determining the structure of this region in micelles using NMR. NMR spectra of unlabelled TM VI-VII peptide show good quality spectra for structure determination. Further experiments with 15N labelled peptide will further define the structure. This will provide insight into TM helix interactions in NHE1 and help us to build up the structure of the protein from these TM segments. (Supported by AHFMR, HSF, CIHR, and AIHS)." @default.
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- W2021125003 date "2011-02-01" @default.
- W2021125003 modified "2023-10-18" @default.
- W2021125003 title "NMR Structural Studies of a Two-Transmembrane Helix Segment of the Na+/H+ Exchanger Isoform 1" @default.
- W2021125003 doi "https://doi.org/10.1016/j.bpj.2010.12.2292" @default.
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