5X1C
Crystal Structure of Human CRMP-2 without C-terminal Tail
5X1C の概要
| エントリーDOI | 10.2210/pdb5x1c/pdb |
| 関連するPDBエントリー | 5X1A 5X1D |
| 分子名称 | Dihydropyrimidinase-related protein 2 (2 entities in total) |
| 機能のキーワード | developmental protein, phosphoprotein, microtubule associated proteins, neurogenesis, dihydropyrimidase-related protein, collapsin response mediator protein, protein binding |
| 由来する生物種 | Homo sapiens (Human) |
| 細胞内の位置 | Cytoplasm, cytosol : Q16555 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 106097.59 |
| 構造登録者 | |
| 主引用文献 | 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 Cited by 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: 28878401DOI: 10.1038/s41598-017-11031-4 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.101 Å) |
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