1PA7

Crystal structure of amino-terminal microtubule binding domain of EB1

1PA7 の概要

• エントリーDOI: 10.2210/pdb1pa7/pdb
• 関連するPDBエントリー: 1UEG
• 分子名称: Microtubule-associated protein RP/EB family member 1, SULFATE ION (3 entities in total)
• 機能のキーワード: ch domain, structural protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytoskeleton: Q15691
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15242.51

構造登録者

Hayashi, I.,Ikura, M. (登録日: 2003-05-13, 公開日: 2003-10-21, 最終更新日: 2024-03-13)

主引用文献

Hayashi, I.,Ikura, M.
Crystal structure of the amino-terminal microtubule-binding domain of end-binding protein 1 (EB1)
J.Biol.Chem., 278:36430-36434, 2003

PubMed Abstract: The end-binding protein 1 (EB1) family is a highly conserved group of proteins that localizes to the plus-ends of microtubules. EB1 has been shown to play an important role in regulating microtubule dynamics and chromosome segregation, but its regulation mechanism is poorly understood. We have determined the 1.45-A resolution crystal structure of the amino-terminal domain of EB1, which is essential for microtubule binding, and show that it forms a calponin homology (CH) domain fold that is found in many proteins involved in the actin cytoskeleton. The functional CH domain for actin binding is a tandem pair, whereas EB1 is the first example of a single CH domain that can associate with the microtubule filament. Although our biochemical study shows that microtubule binding of EB1 is electrostatic in part, our mutational analysis suggests that the hydrophobic network, which is partially exposed in our crystal structure, is also important for the association. We propose that, like other actin-binding CH domains, EB1 employs the hydrophobic interaction to bind to microtubules.

PubMed: 12857735
DOI: 10.1074/jbc.M305773200

実験手法

X-RAY DIFFRACTION (1.45 Å)