5X1C

Crystal Structure of Human CRMP-2 without C-terminal Tail

Summary for 5X1C

• Entry DOI: 10.2210/pdb5x1c/pdb
• Related: 5X1A 5X1D
• Descriptor: Dihydropyrimidinase-related protein 2 (2 entities in total)
• Functional Keywords: developmental protein, phosphoprotein, microtubule associated proteins, neurogenesis, dihydropyrimidase-related protein, collapsin response mediator protein, protein binding
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm, cytosol : Q16555
• Total number of polymer chains: 2
• Total formula weight: 106097.59

Authors

Nitta, R.,Tomabechi, Y.,Aoki, M.,Shirouzu, M. (deposition date: 2017-01-25, release date: 2017-09-20, Last modification date: 2024-03-20)

Primary citation

Niwa, S.,Nakamura, F.,Tomabechi, Y.,Aoki, M.,Shigematsu, H.,Matsumoto, T.,Yamagata, A.,Fukai, S.,Hirokawa, N.,Goshima, Y.,Shirouzu, M.,Nitta, R.
Structural basis for CRMP2-induced axonal microtubule formation
Sci Rep, 7:10681-10681, 2017

PubMed Abstract: Microtubule associated protein Collapsin response mediator protein 2 (CRMP2) regulates neuronal polarity in developing neurons through interactions with tubulins or microtubules. However, how CRMP2 promotes axonal formation by affecting microtubule behavior remains unknown. This study aimed to obtain the structural basis for CRMP2-tubulin/microtubule interaction in the course of axonogenesis. The X-ray structural studies indicated that the main interface to the soluble tubulin-dimer is the last helix H19 of CRMP2 that is distinct from the known C-terminal tail-mediated interaction with assembled microtubules. In vitro structural and functional studies also suggested that the H19-mediated interaction promoted the rapid formation of GTP-state microtubules directly, which is an important feature of the axon. Consistently, the H19 mutants disturbed axon elongation in chick neurons, and failed to authorize the structural features for axonal microtubules in Caenorhabditis elegans. Thus, CRMP2 induces effective axonal microtubule formation through H19-mediated interactions with a soluble tubulin-dimer allowing axonogenesis to proceed.

PubMed: 28878401
DOI: 10.1038/s41598-017-11031-4

Experimental method

X-RAY DIFFRACTION (2.101 Å)