3HAI
Crystal structure of human PACSIN1 F-BAR domain (P21 lattice)
3HAI の概要
| エントリーDOI | 10.2210/pdb3hai/pdb |
| 関連するPDBエントリー | 3HAH 3HAJ |
| 分子名称 | human PACSIN1 F-BAR, CALCIUM ION (3 entities in total) |
| 機能のキーワード | pacsin, syndapin, fap52, f-bar, coiled coil, cytoplasm, endocytosis, phosphoprotein, polymorphism, sh3 domain |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Cytoplasm (By similarity): Q9BY11 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 145580.30 |
| 構造登録者 | Wang, Q.,Navarro, M.V.A.S.,Peng, G.,Rajashankar, K.R.,Sondermann, H. (登録日: 2009-05-01, 公開日: 2009-06-16, 最終更新日: 2024-02-21) |
| 主引用文献 | Wang, Q.,Navarro, M.V.,Peng, G.,Molinelli, E.,Lin Goh, S.,Judson, B.L.,Rajashankar, K.R.,Sondermann, H. Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin. Proc.Natl.Acad.Sci.USA, 106:12700-12705, 2009 Cited by PubMed Abstract: Peripheral membrane proteins of the Bin/amphiphysin/Rvs (BAR) and Fer-CIP4 homology-BAR (F-BAR) family participate in cellular membrane trafficking and have been shown to generate membrane tubules. The degree of membrane bending appears to be encoded in the structure and immanent curvature of the particular protein domains, with BAR and F-BAR domains inducing high- and low-curvature tubules, respectively. In addition, oligomerization and the formation of ordered arrays influences tubule stabilization. Here, the F-BAR domain-containing protein Pacsin was found to possess a unique activity, creating small tubules and tubule constrictions, in addition to the wide tubules characteristic for this subfamily. Based on crystal structures of the F-BAR domain of Pacsin and mutagenesis studies, vesiculation could be linked to the presence of unique structural features distinguishing it from other F-BAR proteins. Tubulation was suppressed in the context of the full-length protein, suggesting that Pacsin is autoinhibited in solution. The regulated deformation of membranes and promotion of tubule constrictions by Pacsin suggests a more versatile function of these proteins in vesiculation and endocytosis beyond their role as scaffold proteins. PubMed: 19549836DOI: 10.1073/pnas.0902974106 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.881 Å) |
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