4PKX
The structure of a conserved Piezo channel domain reveals a novel beta sandwich fold
4PKX の概要
エントリーDOI | 10.2210/pdb4pkx/pdb |
関連するPDBエントリー | 4PKE |
分子名称 | Protein C10C5.1, isoform i (2 entities in total) |
機能のキーワード | mechanosensitive, channel, piezo, membrane protein |
由来する生物種 | Caenorhabditis elegans |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 32953.00 |
構造登録者 | Kamajaya, A.,Kaiser, J.,Lee, J.,Reid, M.,Rees, D.C. (登録日: 2014-05-15, 公開日: 2014-10-08, 最終更新日: 2023-12-27) |
主引用文献 | Kamajaya, A.,Kaiser, J.T.,Lee, J.,Reid, M.,Rees, D.C. The Structure of a Conserved Piezo Channel Domain Reveals a Topologically Distinct beta Sandwich Fold. Structure, 22:1520-1527, 2014 Cited by PubMed Abstract: Piezo has recently been identified as a family of eukaryotic mechanosensitive channels composed of subunits containing over 2,000 amino acids, without recognizable sequence similarity to other channels. Here, we present the crystal structure of a large, conserved extramembrane domain located just before the last predicted transmembrane helix of C. elegans PIEZO, which adopts a topologically distinct β sandwich fold. The structure was also determined of a point mutation located on a conserved surface at the position equivalent to the human PIEZO1 mutation found in dehydrated hereditary stomatocytosis patients (M2225R). While the point mutation does not change the overall domain structure, it does alter the surface electrostatic potential that may perturb interactions with a yet-to-be-identified ligand or protein. The lack of structural similarity between this domain and any previously characterized fold, including those of eukaryotic and bacterial channels, highlights the distinctive nature of the Piezo family of eukaryotic mechanosensitive channels. PubMed: 25242456DOI: 10.1016/j.str.2014.08.009 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.54 Å) |
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