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Catalysis-associated conformational changes revealed by human CD38 complexed with a non-hydrolyzable substrate analog

Qun Liu1, Irina A Kriksunov, Christelle Moreau

  • 1MacCHESS, Cornell High Energy Synchrotron Source, Cornell University, Ithaca, New York 14853, USA.

The Journal of Biological Chemistry
|June 27, 2007
PubMed
Summary

Cyclic ADP-ribose (cADPR) hydrolysis by CD38 is structurally detailed using a non-hydrolyzable analog, N1-cIDPR. This reveals enzyme-substrate conformational changes crucial for calcium signaling and drug design.

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