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PDBsum entry 4qby
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Hydrolase/hydrolase inhibitor
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PDB id
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4qby
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Contents |
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250 a.a.
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244 a.a.
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240 a.a.
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235 a.a.
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231 a.a.
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243 a.a.
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241 a.a.
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226 a.a.
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204 a.a.
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195 a.a.
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212 a.a.
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222 a.a.
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233 a.a.
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196 a.a.
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References listed in PDB file
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Key reference
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Title
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Differential global structural changes in the core particle of yeast and mouse proteasome induced by ligand binding.
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Authors
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M.Arciniega,
P.Beck,
O.F.Lange,
M.Groll,
R.Huber.
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Ref.
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Proc Natl Acad Sci U S A, 2014,
111,
9479-9484.
[DOI no: ]
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PubMed id
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Abstract
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Two clusters of configurations of the main proteolytic subunit β5 were
identified by principal component analysis of crystal structures of the yeast
proteasome core particle (yCP). The apo-cluster encompasses unliganded species
and complexes with nonpeptidic ligands, and the pep-cluster comprises complexes
with peptidic ligands. The murine constitutive CP structures conform to the
yeast system, with the apo-form settled in the apo-cluster and the PR-957 (a
peptidic ligand) complex in the pep-cluster. In striking contrast, the murine
immune CP classifies into the pep-cluster in both the apo and the
PR-957-liganded species. The two clusters differ essentially by multiple small
structural changes and a domain motion enabling enclosure of the peptidic ligand
and formation of specific hydrogen bonds in the pep-cluster. The immune CP
species is in optimal peptide binding configuration also in its apo form. This
favors productive ligand binding and may help to explain the generally increased
functional activity of the immunoproteasome. Molecular dynamics simulations of
the representative murine species are consistent with the experimentally
observed configurations. A comparison of all 28 subunits of the unliganded
species with the peptidic liganded forms demonstrates a greatly enhanced
plasticity of β5 and suggests specific signaling pathways to other subunits.
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