4Q96
CID of human RPRD1B in complex with an unmodified CTD peptide
4Q96 の概要
| エントリーDOI | 10.2210/pdb4q96/pdb |
| 関連するPDBエントリー | 4Q94 |
| 分子名称 | Regulation of nuclear pre-mRNA domain-containing protein 1B, RPB1-CTD, UNKNOWN ATOM OR ION, ... (5 entities in total) |
| 機能のキーワード | protein binding, transcription, structural genomics, structural genomics consortium, sgc |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| 細胞内の位置 | Nucleus: Q9NQG5 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 67033.56 |
| 構造登録者 | Ni, Z.,Xu, C.,Tempel, W.,El Bakkouri, M.,Loppnau, P.,Guo, X.,Bountra, C.,Arrowsmith, C.H.,Edwards, A.M.,Min, J.,Greenblatt, J.F.,Structural Genomics Consortium (SGC) (登録日: 2014-04-29, 公開日: 2014-06-04, 最終更新日: 2025-03-26) |
| 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: 24997600DOI: 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 (1.85 Å) |
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