Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions.

@article{Smith2003StructureOT,
  title={Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions.},
  author={W. James Smith and Nicolas Nassar and Anthony Bretscher and Richard A. Cerione and P. Andrew Karplus},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 7},
  pages={4949-56}
}
Ezrin is a member of the ERM (ezrin, radixin, moesin) family of proteins that cross-link the actin cytoskeleton to the plasma membrane and also may function in signaling cascades that regulate the assembly of actin stress fibers. Here, we report a crystal structure for the free (activated) FERM domain (residues 2-297) of recombinant human ezrin at 2.3 A resolution. Structural comparison among the dormant moesin FERM domain structure and the three known active FERM domain structures (radixin… CONTINUE READING

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