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2PL3

Human DEAD-box RNA helicase DDX10, DEAD domain in complex with ADP

2PL3 の概要
エントリーDOI10.2210/pdb2pl3/pdb
分子名称Probable ATP-dependent RNA helicase DDX10, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
機能のキーワードrna, helicase, dead, structural genomics, structural genomics consortium, sgc, hydrolase
由来する生物種Homo sapiens (human)
タンパク質・核酸の鎖数1
化学式量合計27226.49
構造登録者
主引用文献Schutz, P.,Karlberg, T.,van den Berg, S.,Collins, R.,Lehtio, L.,Hogbom, M.,Holmberg-Schiavone, L.,Tempel, W.,Park, H.W.,Hammarstrom, M.,Moche, M.,Thorsell, A.G.,Schuler, H.
Comparative Structural Analysis of Human DEAD-Box RNA Helicases.
Plos One, 5:12791-12791, 2010
Cited by
PubMed Abstract: DEAD-box RNA helicases play various, often critical, roles in all processes where RNAs are involved. Members of this family of proteins are linked to human disease, including cancer and viral infections. DEAD-box proteins contain two conserved domains that both contribute to RNA and ATP binding. Despite recent advances the molecular details of how these enzymes convert chemical energy into RNA remodeling is unknown. We present crystal structures of the isolated DEAD-domains of human DDX2A/eIF4A1, DDX2B/eIF4A2, DDX5, DDX10/DBP4, DDX18/myc-regulated DEAD-box protein, DDX20, DDX47, DDX52/ROK1, and DDX53/CAGE, and of the helicase domains of DDX25 and DDX41. Together with prior knowledge this enables a family-wide comparative structural analysis. We propose a general mechanism for opening of the RNA binding site. This analysis also provides insights into the diversity of DExD/H- proteins, with implications for understanding the functions of individual family members.
PubMed: 20941364
DOI: 10.1371/journal.pone.0012791
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.15 Å)
構造検証レポート
Validation report summary of 2pl3
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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