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4FLA

Crystal structure of human RPRD1B, carboxy-terminal domain

4FLA の概要
エントリーDOI10.2210/pdb4fla/pdb
分子名称Regulation of nuclear pre-mRNA domain-containing protein 1B, UNKNOWN ATOM OR ION (3 entities in total)
機能のキーワードstructural genomics consortium, sgc, transcription
由来する生物種Homo sapiens (human)
細胞内の位置Nucleus: Q9NQG5
タンパク質・核酸の鎖数4
化学式量合計69462.70
構造登録者
主引用文献Ni, Z.,Xu, C.,Guo, X.,Hunter, G.O.,Kuznetsova, O.V.,Tempel, W.,Marcon, E.,Zhong, G.,Guo, H.,Kuo, W.H.,Li, J.,Young, P.,Olsen, J.B.,Wan, C.,Loppnau, P.,El Bakkouri, M.,Senisterra, G.A.,He, H.,Huang, H.,Sidhu, S.S.,Emili, A.,Murphy, S.,Mosley, A.L.,Arrowsmith, C.H.,Min, J.,Greenblatt, J.F.
RPRD1A and RPRD1B are human RNA polymerase II C-terminal domain scaffolds for Ser5 dephosphorylation.
Nat.Struct.Mol.Biol., 21:686-695, 2014
Cited by
PubMed Abstract: The RNA polymerase II (RNAPII) C-terminal domain (CTD) heptapeptide repeats (1-YSPTSPS-7) undergo dynamic phosphorylation and dephosphorylation during the transcription cycle to recruit factors that regulate transcription, RNA processing and chromatin modification. We show here that RPRD1A and RPRD1B form homodimers and heterodimers through their coiled-coil domains and interact preferentially via CTD-interaction domains (CIDs) with RNAPII CTD repeats phosphorylated at S2 and S7. Crystal structures of the RPRD1A, RPRD1B and RPRD2 CIDs, alone and in complex with RNAPII CTD phosphoisoforms, elucidate the molecular basis of CTD recognition. In an example of cross-talk between different CTD modifications, our data also indicate that RPRD1A and RPRD1B associate directly with RPAP2 phosphatase and, by interacting with CTD repeats where phospho-S2 and/or phospho-S7 bracket a phospho-S5 residue, serve as CTD scaffolds to coordinate the dephosphorylation of phospho-S5 by RPAP2.
PubMed: 24997600
DOI: 10.1038/nsmb.2853
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.2 Å)
構造検証レポート
Validation report summary of 4fla
検証レポート(詳細版)ダウンロードをダウンロード

250059

件を2026-03-04に公開中

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