2QK2

Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1

2QK2 の概要

• エントリーDOI: 10.2210/pdb2qk2/pdb
• 関連するPDBエントリー: 2QJX 2QJZ 2QK0 2QK1
• 分子名称: LP04448p (2 entities in total)
• 機能のキーワード: mini spindles, msps, xmap215, dis1, stu2, heat repeat, microtubule plus end, +tip, protein binding
• 由来する生物種: Drosophila melanogaster (fruit fly)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26762.62

構造登録者

Slep, K.C.,Vale, R.D. (登録日: 2007-07-10, 公開日: 2007-10-02, 最終更新日: 2024-10-30)

主引用文献

Slep, K.C.,Vale, R.D.
Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170, and EB1.
Mol.Cell, 27:976-991, 2007

PubMed Abstract: Microtubule plus end binding proteins (+TIPs) localize to the dynamic plus ends of microtubules, where they stimulate microtubule growth and recruit signaling molecules. Three main +TIP classes have been identified (XMAP215, EB1, and CLIP-170), but whether they act upon microtubule plus ends through a similar mechanism has not been resolved. Here, we report crystal structures of the tubulin binding domains of XMAP215 (yeast Stu2p and Drosophila Msps), EB1 (yeast Bim1p and human EB1), and CLIP-170 (human), which reveal diverse tubulin binding interfaces. Functional studies, however, reveal a common property that native or artificial dimerization of tubulin binding domains (including chemically induced heterodimers of EB1 and CLIP-170) induces tubulin nucleation/assembly in vitro and, in most cases, plus end tracking in living cells. We propose that +TIPs, although diverse in structure, share a common property of multimerizing tubulin, thus acting as polymerization chaperones that aid in subunit addition to the microtubule plus end.

PubMed: 17889670
DOI: 10.1016/j.molcel.2007.07.023

実験手法

X-RAY DIFFRACTION (2.1 Å)