Journal article

Interaction of N-terminal peptide analogues of the Na ,K -ATPase with membranes

K Nguyen, A Garcia, MA Sani, D Diaz, V Dubey, D Clayton, G Dal Poggetto, F Cornelius, RJ Payne, F Separovic, H Khandelia, RJ Clarke

Biochimica Et Biophysica Acta Biomembranes | Published : 2018

Abstract

The Na+,K+-ATPase, which is present in the plasma membrane of all animal cells, plays a crucial role in maintaining the Na+ and K+ electrochemical potential gradients across the membrane. Recent studies have suggested that the N-terminus of the protein's catalytic α-subunit is involved in an electrostatic interaction with the surrounding membrane, which controls the protein's conformational equilibrium. However, because the N-terminus could not yet be resolved in any X-ray crystal structures, little information about this interaction is so far available. In measurements utilising poly-L-lysine as a model of the protein's lysine-rich N-terminus and using lipid vesicles of defined composition,..

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University of Melbourne Researchers

Grants

Awarded by Australian Research Council


Funding Acknowledgements

R. J. C. and F.S. acknowledge with gratitude financial support from the Australian Research Council (Discovery Grants No. DP121003548, DP150101112 and DP170101732 to R. J. C. and DP140102127 to F.S). The simulations were carried out on the Danish e-Infrastructure Cooperation (DeiC) National HPC Center with ABACUS 2.0, and on the Swiss PizDaint Supercomputer under the PRACE 14th Call, number 2016153468. H. K. and V. D. acknowledge financial support from the Lundbeckfonden.