Structure of human collapsin response mediator protein 1: A possible role of its C-terminal tail
Journal
Acta Crystallographica Section:F Structural Biology Communications
Journal Volume
71
Pages
938-945
Date Issued
2015
Author(s)
Abstract
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 3Å. 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.
SDGs
Publisher
International Union of Crystallography
Type
journal article