2N1A

Docked structure between SUMO1 and ZZ-domain from CBP

2N1A の概要

• エントリーDOI: 10.2210/pdb2n1a/pdb
• NMR情報: BMRB: 25553
• 分子名称: Small ubiquitin-related modifier 1, CREB-binding protein, ZINC ION (3 entities in total)
• 機能のキーワード: protein-protein complex, docked structure, sumo1, sim, zz-domain, transcription
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18165.07

構造登録者

Diehl, C. (登録日: 2015-03-26, 公開日: 2016-05-04, 最終更新日: 2024-05-01)

主引用文献

Diehl, C.,Akke, M.,Bekker-Jensen, S.,Mailand, N.,Streicher, W.,Wikstrom, M.
Structural Analysis of a Complex between Small Ubiquitin-like Modifier 1 (SUMO1) and the ZZ Domain of CREB-binding Protein (CBP/p300) Reveals a New Interaction Surface on SUMO.
J.Biol.Chem., 291:12658-12672, 2016

PubMed Abstract: We have recently discovered that the ZZ zinc finger domain represents a novel small ubiquitin-like modifier (SUMO) binding motif. In this study we identify the binding epitopes in the ZZ domain of CBP (CREB-binding protein) and SUMO1 using NMR spectroscopy. The binding site on SUMO1 represents a unique epitope for SUMO interaction spatially opposite to that observed for canonical SUMO interaction motifs (SIMs). HADDOCK docking simulations using chemical shift perturbations and residual dipolar couplings was employed to obtain a structural model for the ZZ domain-SUMO1 complex. Isothermal titration calorimetry experiments support this model by showing that the mutation of key residues in the binding site abolishes binding and that SUMO1 can simultaneously and non-cooperatively bind both the ZZ domain and a canonical SIM motif. The binding dynamics of SUMO1 was further characterized using (15)N Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersions, which define the off rates for the ZZ domain and SIM motif and show that the dynamic binding process has different characteristics for the two cases. Furthermore, in the absence of bound ligands SUMO1 transiently samples a high energy conformation, which might be involved in ligand binding.

PubMed: 27129204
DOI: 10.1074/jbc.M115.711325

実験手法

SOLUTION NMR