1V8K

The Crystal Structure of the Minimal Functional Domain of the Microtubule Destabilizer KIF2C Complexed with Mg-AMPPNP

1V8K の概要

• エントリーDOI: 10.2210/pdb1v8k/pdb
• 関連するPDBエントリー: 1V8J
• 分子名称: Kinesin-like protein KIF2C, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: kinesin-like protein, microtubule destabilizer, structural protein
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cytoplasm, cytoskeleton (By similarity): Q922S8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47333.21

構造登録者

Ogawa, T.,Nitta, R.,Okada, Y.,Hirokawa, N. (登録日: 2004-01-09, 公開日: 2004-03-02, 最終更新日: 2023-12-27)

主引用文献

Ogawa, T.,Nitta, R.,Okada, Y.,Hirokawa, N.
A common mechanism for microtubule destabilizers-M type kinesins stabilize curling of the protofilament using the class-specific neck and loops.
Cell(Cambridge,Mass.), 116:591-602, 2004

PubMed Abstract: Unlike other kinesins, middle motor domain-type kinesins depolymerize the microtubule from its ends. To elucidate its mechanism, we solved the X-ray crystallographic structure of KIF2C, a murine member of this family. Three major class-specific features were identified. The class-specific N-terminal neck adopts a long and rigid helical structure extending out vertically into the interprotofilament groove. This structure explains its dual roles in targeting to the end of the microtubule and in destabilization of the lateral interaction of the protofilament. The loop L2 forms a unique finger-like structure, long and rigid enough to reach the next tubulin subunit to stabilize the peeling of the protofilament. The open conformation of the switch I loop could be reversed by the shift of the microtubule binding L8 loop, suggesting its role as the sensor to trigger ATP hydrolysis. Mutational analysis supports these structural implications.

PubMed: 14980225
DOI: 10.1016/S0092-8674(04)00129-1

実験手法

X-RAY DIFFRACTION (2.25 Å)