5TBX
hnRNP A18 RNA Recognition Motif
5TBX の概要
| エントリーDOI | 10.2210/pdb5tbx/pdb |
| 分子名称 | Cold-inducible RNA-binding protein, ACETATE ION, NICKEL (II) ION, ... (4 entities in total) |
| 機能のキーワード | rna-binding protein, rna binding protein |
| 由来する生物種 | Homo sapiens (Human) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 20460.19 |
| 構造登録者 | Coburn, K.M.,Melville, Z.,Aligholizadeh, E.,Roth, B.M.,Varney, K.M.,Weber, D.J. (登録日: 2016-09-13, 公開日: 2017-04-12, 最終更新日: 2024-04-03) |
| 主引用文献 | Coburn, K.,Melville, Z.,Aligholizadeh, E.,Roth, B.M.,Varney, K.M.,Carrier, F.,Pozharski, E.,Weber, D.J. Crystal structure of the human heterogeneous ribonucleoprotein A18 RNA-recognition motif. Acta Crystallogr F Struct Biol Commun, 73:209-214, 2017 Cited by PubMed Abstract: The heterogeneous ribonucleoprotein A18 (hnRNP A18) is upregulated in hypoxic regions of various solid tumors and promotes tumor growth via the coordination of mRNA transcripts associated with pro-survival genes. Thus, hnRNP A18 represents an important therapeutic target in tumor cells. Presented here is the first X-ray crystal structure to be reported for the RNA-recognition motif of hnRNP A18. By comparing this structure with those of homologous RNA-binding proteins (i.e. hnRNP A1), three residues on one face of an antiparallel β-sheet (Arg48, Phe50 and Phe52) and one residue in an unstructured loop (Arg41) were identified as likely to be involved in protein-nucleic acid interactions. This structure helps to serve as a foundation for biophysical studies of this RNA-binding protein and structure-based drug-design efforts for targeting hnRNP A18 in cancer, such as malignant melanoma, where hnRNP A18 levels are elevated and contribute to disease progression. PubMed: 28368279DOI: 10.1107/S2053230X17003454 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.767 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






