1DT4
CRYSTAL STRUCTURE OF NOVA-1 KH3 K-HOMOLOGY RNA-BINDING DOMAIN
1DT4 の概要
エントリーDOI | 10.2210/pdb1dt4/pdb |
関連するPDBエントリー | 1DTJ 1EC6 |
分子名称 | NEURO-ONCOLOGICAL VENTRAL ANTIGEN 1 (1 entity in total) |
機能のキーワード | kh domain, alpha-beta fold, rna-binding motif, immune system |
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 | 7895.20 |
構造登録者 | Lewis, H.A.,Chen, H.,Edo, C.,Buckanovich, R.J.,Yang, Y.Y.L. (登録日: 2000-01-11, 公開日: 2000-02-11, 最終更新日: 2024-02-07) |
主引用文献 | Lewis, H.A.,Chen, H.,Edo, C.,Buckanovich, R.J.,Yang, Y.Y.,Musunuru, K.,Zhong, R.,Darnell, R.B.,Burley, S.K. Crystal structures of Nova-1 and Nova-2 K-homology RNA-binding domains. Structure Fold.Des., 7:191-203, 1999 Cited by PubMed Abstract: Nova-1 and Nova-2 are related neuronal proteins that were initially cloned using antisera obtained from patients with the autoimmune neurological disease paraneoplastic opsoclonus-myoclonus ataxia (POMA). Both of these disease gene products contain three RNA-binding motifs known as K-homology or KH domains, and their RNA ligands have been identified via binding-site selection experiments. The KH motif structure has been determined previously using NMR spectroscopy, but not using X-ray crystallography. Many proteins contain more than one KH domain, yet there is no published structural information regarding the behavior of such multimers. PubMed: 10368286DOI: 10.1016/S0969-2126(99)80025-2 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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