Collapsin response mediator protein 1 (CRMP-1) is the first identified member of the CRMP family and is crucial for both the mediation of neuronal differentiation and in suppressing the invasion of lung cancer. The crystal structure of full-length human CRMP-1 was determined at a resolution of 3 Å. Human CRMP-1 comprises a tetrameric assembly; its overall structure is similar to that of mouse CRMP-1, but the measured electron density of the C-terminal residues 488-496 show a randomly coiled link that connects the protomers to each other, within which residues 497-572 are proteolytically susceptible in vivo. Deletion of residues 472-572 by thrombin in vitro not only releases a randomly coiled tail but also transduces observable structural changes of CRMP-1, as revealed by analytical size-exclusive chromatography and circular dichroism spectra. These results indicate a possible alternative role in CRMP dynamics and function.
