Dear Jacob, The protease thrombin is another example. Thrombin is activated by Na+ (but not Li+ or K+). We have shown using NMR that Na+ binding allosterically stabilizes active conformations of thrombin. Additionally, numerous crystal structures of Na+-free (“slow” thrombin) and Na+-bound (“fast” thrombin) have been published.
These publications should give you a good overview: https://www.ncbi.nlm.nih.gov/pubmed/20660315 https://www.ncbi.nlm.nih.gov/pubmed/22944689 http://www.pnas.org/content/100/24/13785/T1.expansion.html Best, Bernhard Bernhard C. Lechtenberg, PhD Postdoctoral Associate Riedl Lab Cancer Metabolism and Signaling Networks Program NCI-Designated Cancer Center [cid:24A04CE0-5418-4257-A8D1-8084CA766BC9@burnham.org] 10901 N. Torrey Pines Road, La Jolla, CA 92037 T 858.646.3100 ext. 4216 E blechtenb...@sbpdiscovery.org<mailto:blechtenb...@sbpdiscovery.org> Science Benefiting Patients® On Jan 9, 2018, at 6:42 AM, Keller, Jacob <kell...@janelia.hhmi.org<mailto:kell...@janelia.hhmi.org>> wrote: Dear Crystallographers, Is anyone aware of a soluble protein which changes large-scale conformation +/- Na+, and is specific for Na+ per se, or at least ignores K+ and Ca++? E.g., Rb+ or Li+ might be okay. Structural info would be a plus, but not a sine qua non. Similarly, what about with K+ or Cl- specificities, but oblivious to similar common ions? All the best, Jacob Keller +++++++++++++++++++++++++++++++++++++++++++++++++ Jacob Pearson Keller Research Scientist / Looger Lab HHMI Janelia Research Campus 19700 Helix Dr, Ashburn, VA 20147 (571)209-4000 x3159 +++++++++++++++++++++++++++++++++++++++++++++++++ The content of this email is confidential and intended for the recipient specified in message only. It is strictly forbidden to share any part of this message with any third party, without a written consent of the sender. If you received this message by mistake, please reply to this message and follow with its deletion, so that we can ensure such a mistake does not occur in the future.
