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1SJR

NMR Structure of RRM2 from Human Polypyrimidine Tract Binding Protein Isoform 1 (PTB1)

1SJR の概要
エントリーDOI10.2210/pdb1sjr/pdb
関連するPDBエントリー1sjq
NMR情報BMRB: 6177
分子名称Polypyrimidine tract-binding protein 1 (1 entity in total)
機能のキーワードextended babbab motif, rna binding protein
由来する生物種Homo sapiens (human)
細胞内の位置Nucleus: P26599
タンパク質・核酸の鎖数1
化学式量合計17758.07
構造登録者
主引用文献Simpson, P.J.,Monie, T.P.,Szendroi, A.,Davydova, N.,Tyzack, J.K.,Conte, M.R.,Read, C.M.,Cary, P.D.,Svergun, D.I.,Konarev, P.V.,Curry, S.,Matthews, S.J.
Structure and RNA Interactions of the N-Terminal RRM Domains of PTB
Structure, 12:1631-1643, 2004
Cited by
PubMed Abstract: The polypyrimidine tract binding protein (PTB) is an important regulator of alternative splicing that also affects mRNA localization, stabilization, polyadenylation, and translation. NMR structural analysis of the N-terminal half of PTB (residues 55-301) shows a canonical structure for RRM1 but reveals novel extensions to the beta strands and C terminus of RRM2 that significantly modify the beta sheet RNA binding surface. Although PTB contains four RNA recognition motifs (RRMs), it is widely held that only RRMs 3 and 4 are involved in RNA binding and that RRM2 mediates homodimerization. However, we show here not only that the RRMs 1 and 2 contribute substantially to RNA binding but also that full-length PTB is monomeric, with an elongated structure determined by X-ray solution scattering that is consistent with a linear arrangement of the constituent RRMs. These new insights into the structure and RNA binding properties of PTB suggest revised models of its mechanism of action.
PubMed: 15341728
DOI: 10.1016/j.str.2004.07.008
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 1sjr
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2026-04-22に公開中

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