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Skip to Search Results- 3Escherichia-Coli
- 3Lactose Permease
- 3Protein Secondary Structure
- 2Chemical-Shift Index
- 2Cysteine-Scanning Mutagenesis
- 2Helix
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Structural and functional characterization of transmembrane segment IV of the NHE1 isoform of the na+/H+ exchanger
Download2005-01-01
Slepkov, Emily R., Rainey, Jan K., Li, Xiuju J., Liu, Yonghsheng S., Cheng, Florence J., Lindhout, Darrin A., Sykes, Brian D., Fliegel, Larry
The Na+/H+ exchanger isoform 1 is a ubiquitously expressed integral membrane protein that regulates intracellular pH in mammals. We characterized the structural and functional aspects of the critical transmembrane (TM) segment IV. Each residue was mutated to cysteine in cysteine-less NHE1. TM IV...
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Structural and functional characterization of transmembrane segment IX of the NHE1 isoform of the na(+)/H(+) exchanger
Download2008-01-01
Reddy, Tyler, Ding, Jie, Li, Xiuju J., Sykes, Brian D., Rainey, Jan K., Fliegel, Larry
The Na+/H+ exchanger isoform 1 (NHE1) is an integral membrane protein that regulates intracellular pH by removing one intracellular H+ in exchange for one extracellular Na+. It has a large N-terminal membrane domain of 12 transmembrane segments and an intracellular C-terminal regulatory domain....
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Structural and functional characterization of transmembrane segment VII of the na+/H+ exchanger isoform 1
Download2006-01-01
Ding, Jie, Rainey, Jan K., Xu, Caroline, Sykes, Brian D., Fliegel, Larry
The Na+/H+ exchanger isoform 1 is an integral membrane protein that regulates intracellular pH by exchanging one intracellular H+ for one extracellular Na+. It is composed of an N-terminal membrane domain of 12 transmembrane segments and an intracellular C-terminal regulatory domain. We...
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Transmembrane segment XI of the na+/H+ antiporter of S. pombe is a critical part of the ion translocation pore
Download2017-01-01
Dutta, Debajyoti, Shin, Kyungsoo, Rainey, Jan K., Fliegel, Larry
The Na+/H+ exchanger of the plasma membrane of S. pombe (SpNHE1) removes intracellular sodium in exchange for an extracellular proton. We examined the structure and functional role of amino acids 360–393 of putative transmembrane (TM) segment XI of SpNHE1. Structural analysis suggested that it...