The extended transmembrane orai1 N-terminal (ETON) region combines binding interface and gate for orai1 activation by STIM1

97Citations
Citations of this article
82Readers
Mendeley users who have this article in their library.

This article is free to access.

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.

Cite

CITATION STYLE

APA

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

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free