3ACO

Crystal structure of the EFC/F-BAR domain of human PACSIN2/Syndapin II (2.7 A)

3ACO の概要

• エントリーDOI: 10.2210/pdb3aco/pdb
• 関連するPDBエントリー: 3ABH
• 分子名称: Protein kinase C and casein kinase substrate in neurons protein 2, CALCIUM ION (3 entities in total)
• 機能のキーワード: helix bundle, coiled-coil, endocytosis
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : Q9UNF0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 82141.38

構造登録者

Shimada, A.,Shirouzu, M.,Hanawa-Suetsugu, K.,Terada, T.,Umehara, T.,Suetsugu, S.,Yamamoto, M.,Yokoyama, S. (登録日: 2010-01-07, 公開日: 2010-04-14, 最終更新日: 2024-10-23)

主引用文献

Shimada, A.,Takano, K.,Shirouzu, M.,Hanawa-Suetsugu, K.,Terada, T.,Toyooka, K.,Umehara, T.,Yamamoto, M.,Yokoyama, S.,Suetsugu, S.
Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II
Febs Lett., 584:1111-1118, 2010

PubMed Abstract: The extended Fes-CIP4 homology (EFC)/FCH-BAR (F-BAR) domain tubulates membranes. Overexpression of the pacsin2 EFC/F-BAR domain resulted in tubular localization inside cells and deformed liposomes into tubules in vitro. We found that overexpression of the pacsin2 EFC/F-BAR domain induced cellular microspikes, with the pacsin2 EFC/F-BAR domain concentrated at the neck. The hydrophobic loops and the basic amino-acid residues on the concave surface of the pacsin2 EFC/F-BAR domain are essential for both the microspike formation and tubulation. Since the curvature of the neck of the microspike and that of the tubulation share similar geometry, the pacsin2 EFC/F-BAR domain is considered to facilitate both microspike formation and tubulation.

PubMed: 20188097
DOI: 10.1016/j.febslet.2010.02.058

実験手法

X-RAY DIFFRACTION (2.7 Å)