2N1A

Docked structure between SUMO1 and ZZ-domain from CBP

Summary for 2N1A

• Entry DOI: 10.2210/pdb2n1a/pdb
• NMR Information: BMRB: 25553
• Descriptor: Small ubiquitin-related modifier 1, CREB-binding protein, ZINC ION (3 entities in total)
• Functional Keywords: protein-protein complex, docked structure, sumo1, sim, zz-domain, transcription
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 18165.07

Authors

Diehl, C. (deposition date: 2015-03-26, release date: 2016-05-04, Last modification date: 2024-05-01)

Primary citation

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

Experimental method

SOLUTION NMR