4WJP

Crystal Structure of SUMO1 in complex with phosphorylated Daxx

4WJP の概要

• エントリーDOI: 10.2210/pdb4wjp/pdb
• 関連するPDBエントリー: 4WJN 4WJO 4WJQ
• 分子名称: Small ubiquitin-related modifier 1, Daxx (3 entities in total)
• 機能のキーワード: sumo1, daxx, sumo interaction motif, phosphosim, protein binding-signaling protein complex, protein binding/signaling protein
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus membrane: P63165
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 23055.30

構造登録者

Cappadocia, L.,Mascle, X.H.,Bourdeau, V.,Tremblay-Belzile, S.,Chaker-Margot, M.,Lussier-Price, M.,Wada, J.,Sakaguchi, K.,Aubry, M.,Ferbeyre, G.,Omichinski, J.G. (登録日: 2014-10-01, 公開日: 2014-12-31, 最終更新日: 2024-10-30)

主引用文献

Cappadocia, L.,Mascle, X.H.,Bourdeau, V.,Tremblay-Belzile, S.,Chaker-Margot, M.,Lussier-Price, M.,Wada, J.,Sakaguchi, K.,Aubry, M.,Ferbeyre, G.,Omichinski, J.G.
Structural and Functional Characterization of the Phosphorylation-Dependent Interaction between PML and SUMO1.
Structure, 23:126-138, 2015

PubMed Abstract: PML and several other proteins localizing in PML-nuclear bodies (PML-NB) contain phosphoSIMs (SUMO-interacting motifs), and phosphorylation of this motif plays a key role in their interaction with SUMO family proteins. We examined the role that phosphorylation plays in the binding of the phosphoSIMs of PML and Daxx to SUMO1 at the atomic level. The crystal structures of SUMO1 bound to unphosphorylated and tetraphosphorylated PML-SIM peptides indicate that three phosphoserines directly contact specific positively charged residues of SUMO1. Surprisingly, the crystal structure of SUMO1 bound to a diphosphorylated Daxx-SIM peptide indicate that the hydrophobic residues of the phosphoSIM bind in a manner similar to that seen with PML, but important differences are observed when comparing the phosphorylated residues. Together, the results provide an atomic level description of how specific acetylation patterns within different SUMO family proteins can work together with phosphorylation of phosphoSIM's regions of target proteins to regulate binding specificity.

PubMed: 25497731
DOI: 10.1016/j.str.2014.10.015

実験手法

X-RAY DIFFRACTION (1.7 Å)