2L9S

Solution structure of Pf1 SID1-mSin3A PAH2 Complex

2L9S の概要

• エントリーDOI: 10.2210/pdb2l9s/pdb
• 関連するPDBエントリー: 1S5Q 1S5R
• NMR情報: BMRB: 17485
• 分子名称: PHD finger protein 12, Paired amphipathic helix protein Sin3a (2 entities in total)
• 機能のキーワード: protein-peptide complex, amphipathic helix motif, transcription
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: Q96QT6 Q60520
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 15810.48

構造登録者

Senthil Kumar, G.,Xie, T.,Zhang, Y.,Radhakrishnan, I. (登録日: 2011-02-23, 公開日: 2011-05-11, 最終更新日: 2024-05-15)

主引用文献

Kumar, G.S.,Xie, T.,Zhang, Y.,Radhakrishnan, I.
Solution Structure of the mSin3A PAH2-Pf1 SID1 Complex: A Mad1/Mxd1-Like Interaction Disrupted by MRG15 in the Rpd3S/Sin3S Complex.
J.Mol.Biol., 408:987-1000, 2011

PubMed Abstract: Histone deacetylation constitutes an important mechanism for silencing genes. The histone-deacetylase-associated mammalian Rpd3S/Sin3S corepressor complex plays key roles in repressing aberrant gene transcription from cryptic transcription initiation sites and in mitigating RNA polymerase II progression in intragenic regions of actively transcribed genes. The Sin3 corepressor functions as a molecular adaptor linking histone deacetylases on the one hand, with the chromatin targeting subunits Pf1 and MRG15 on the other. Pf1 also functions as an adaptor by interacting with MRG15 and engaging in multivalent interactions with Sin3 targeting among other domains the two N-terminal paired amphipathic helix (PAH) domains that serve as sites of interaction with sequence-specific DNA-binding transcription factors. Here, we structurally and functionally evaluate the interaction between the PAH2 domain of mSin3A and the Sin3 interaction domain 1 (SID1) motif of Pf1 and find the structural aspects to be reminiscent of the interaction between the Mad1/Mxd1 transcription factor and Sin3. Pf1 residues within a highly conserved sequence motif immediately C-terminal to SID1 appear not to be important for the interaction with Sin3 PAH2. Unexpectedly, the MRG15 subunit competes, rather than collaborates, with Sin3 for the Pf1 segment encompassing the two conserved motifs, implying competition between two subunits for another subunit of the same chromatin-modifying complex.

PubMed: 21440557
DOI: 10.1016/j.jmb.2011.03.043

実験手法

SOLUTION NMR