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PDBsum entry 3ehv
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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 probing of zn(ii), Cd(ii) and hg(ii) binding to human ubiquitin.
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Authors
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G.Falini,
S.Fermani,
G.Tosi,
F.Arnesano,
G.Natile.
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Ref.
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Chem Commun (camb), 2008,
45,
5960-5962.
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PubMed id
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Abstract
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A structural investigation performed on adducts of human ubiquitin with group-12
metal ions reveals common preferential anchoring sites, the most populated one
being His68; at higher metal ion concentration a second and a third site, close
to the N-terminus of the protein, become populated and promote a polymorphic
transition from orthorhombic to cubic form; Glu16 and Glu18, involved in the
latter metal binding, undergo a remarkable displacement from their position in
native ubiquitin; the aggregate stereochemistry appears to be driven by the
clustering of deshielded backbone hydrogen-bond patches, and metal ions foster
this process.
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