Abstract
Background:STIM1 and Orai1, reconstituting a main cellular Ca2+ entry pathway, interact via their cytosolic strands. Results:The extended transmembrane Orai1 N-terminal (ETON) region combines binding interface and gate for Orai1 activation by STIM1. Conclusion:Several "hot spot" residues in the ETON region mediate STIM1 interaction, enabling conformational reorientation of the gate. Significance: Identification of critical residues for protein-protein interaction are fundamental to therapeutic drug development. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Derler, I., Plenk, P., Fahrner, M., Muik, M., Jardin, I., Schindl, R., … Romanin, C. (2013). The extended transmembrane orai1 N-terminal (ETON) region combines binding interface and gate for orai1 activation by STIM1. Journal of Biological Chemistry, 288(40), 29025–29034. https://doi.org/10.1074/jbc.M113.501510
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