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PDBsum entry 2n1a
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Transcription
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PDB id
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2n1a
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References listed in PDB file
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Key reference
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Title
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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.
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Authors
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C.Diehl,
M.Akke,
S.Bekker-Jensen,
N.Mailand,
W.Streicher,
M.Wikström.
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Ref.
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J Biol Chem, 2016,
291,
12658-12672.
[DOI no: ]
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PubMed id
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Abstract
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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.
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