4OVA
Structure of the two tandem Tudor domains and a new identified KH0 domain from human Fragile X Mental Retardation Protein
4OVA の概要
| エントリーDOI | 10.2210/pdb4ova/pdb |
| 関連するPDBエントリー | 2qnd |
| 分子名称 | Fragile X mental retardation protein 1, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total) |
| 機能のキーワード | kh domain, fragile x mental retardation protein, fmrp, tandem tudor domains, eukaryotic kh domains, kh0 domain, rna binding protein, protein interaction |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Cytoplasm: Q06787 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 97495.18 |
| 構造登録者 | |
| 主引用文献 | Hu, Y.,Chen, Z.H.,Fu, Y.,He, Q.,Jiang, L.,Zheng, J.,Gao, Y.,Mei, P.,Chen, Z.Z.,Ren, X. The amino-terminal structure of human fragile X mental retardation protein obtained using precipitant-immobilized imprinted polymers Nat Commun, 6:6634-6634, 2015 Cited by PubMed Abstract: Flexibility is an intrinsic property of proteins and essential for their biological functions. However, because of structural flexibility, obtaining high-quality crystals of proteins with heterogeneous conformations remain challenging. Here, we show a novel approach to immobilize traditional precipitants onto molecularly imprinted polymers (MIPs) to facilitate protein crystallization, especially for flexible proteins. By applying this method, high-quality crystals of the flexible N-terminus of human fragile X mental retardation protein are obtained, whose absence causes the most common inherited mental retardation. A novel KH domain and an intermolecular disulfide bond are discovered, and several types of dimers are found in solution, thus providing insights into the function of this protein. Furthermore, the precipitant-immobilized MIPs (piMIPs) successfully facilitate flexible protein crystal formation for five model proteins with increased diffraction resolution. This highlights the potential of piMIPs for the crystallization of flexible proteins. PubMed: 25799254DOI: 10.1038/ncomms7634 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3 Å) |
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