TY - JOUR
T1 - Revealing the ligand binding site of NhaA Na+/H+ antiporter and its pH dependence
AU - Maes, Michal
AU - Rimon, Abraham
AU - Kozachkov-Magrisso, Lena
AU - Friedler, Assaf
AU - Padan, Etana
PY - 2012/11/2
Y1 - 2012/11/2
N2 - Background: Cell pH and Na+ homeostasis requires Na +/H+ antiporters such as NhaA. Results: Mutational analysis and ITC measurements revealed the NhaA-Li+ binding site. Conclusion: Binding of Li+ to purified NhaA is enthalpy-driven, highly specific, and pH-dependent and involves a single binding site. Significance: The pH-dependent NhaA-ligand binding is an insight into the mechanism of activity of NhaA and possibly other antiporters.
AB - Background: Cell pH and Na+ homeostasis requires Na +/H+ antiporters such as NhaA. Results: Mutational analysis and ITC measurements revealed the NhaA-Li+ binding site. Conclusion: Binding of Li+ to purified NhaA is enthalpy-driven, highly specific, and pH-dependent and involves a single binding site. Significance: The pH-dependent NhaA-ligand binding is an insight into the mechanism of activity of NhaA and possibly other antiporters.
UR - http://www.scopus.com/inward/record.url?scp=84868306588&partnerID=8YFLogxK
U2 - 10.1074/jbc.M112.391128
DO - 10.1074/jbc.M112.391128
M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???
C2 - 22915592
AN - SCOPUS:84868306588
SN - 0021-9258
VL - 287
SP - 38150
EP - 38157
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 45
ER -