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5X1C

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

5X1C の概要
エントリーDOI10.2210/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
Nitta, R.,Tomabechi, Y.,Aoki, M.,Shirouzu, M. (登録日: 2017-01-25, 公開日: 2017-09-20, 最終更新日: 2024-03-20)
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: 28878401
DOI: 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)
構造検証レポート
Validation report summary of 5x1c
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-10-29に公開中

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