Background: Calmodulin (CaM) is recruited into the death-inducing signaling complex in cholangiocarcinoma cells. Results: CaM binds to FasDD in a 2:1 CaM:FasDD model. CaM antagonists abolish FasDD-CaM interactions. Conclusion: Data offer a structural basis for Fas-CaM interactions and mechanisms of inhibition. Significance: Elucidating the structural determinants of Fas-CaM interaction is critical to understanding the functional role of CaM in Fas-mediated apoptosis. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
