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PDBsum entry 4xkh
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Ubiquitin-binding protein
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PDB id
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4xkh
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Contents |
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72 a.a.
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43 a.a.
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40 a.a.
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76 a.a.
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PDB id:
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| Name: |
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Ubiquitin-binding protein
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Title:
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Crystal structure of the airapl tandem uims in complex with a lys48- linked tri-ubiquitin
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Structure:
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Polyubiquitin-c. Chain: a, f, b, d, g, i. Fragment: unp residues 77-152. Engineered: yes. An1-type zinc finger protein 2b. Chain: e, c, h. Fragment: unp residues 187-240. Synonym: arsenite-inducible RNA-associated protein-like protein, airap-like protein.
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Source:
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Bos taurus. Bovine. Organism_taxid: 9913. Gene: ubc. Expressed in: bos taurus. Expression_system_taxid: 9913. Expression_system_cell: erythrocyte. Mus musculus. Mouse.
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Resolution:
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3.00Å
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R-factor:
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0.203
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R-free:
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0.255
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Authors:
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S.Rahighi,M.Kawasaki,A.Stanhill,S.Wakatsuki
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Key ref:
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S.Rahighi
et al.
(2016).
Selective Binding of AIRAPL Tandem UIMs to Lys48-Linked Tri-Ubiquitin Chains.
Structure,
24,
412-422.
PubMed id:
DOI:
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Date:
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11-Jan-15
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Release date:
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17-Feb-16
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PROCHECK
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Headers
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References
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P0CH28
(UBC_BOVIN) -
Polyubiquitin-C from Bos taurus
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Seq:
Struc:
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690 a.a.
72 a.a.
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Q91X58
(ZFN2B_MOUSE) -
AN1-type zinc finger protein 2B from Mus musculus
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Seq:
Struc:
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257 a.a.
43 a.a.
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DOI no:
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Structure
24:412-422
(2016)
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PubMed id:
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Selective Binding of AIRAPL Tandem UIMs to Lys48-Linked Tri-Ubiquitin Chains.
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S.Rahighi,
I.Braunstein,
N.Ternette,
B.Kessler,
M.Kawasaki,
R.Kato,
T.Matsui,
T.M.Weiss,
A.Stanhill,
S.Wakatsuki.
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ABSTRACT
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Lys48-linked ubiquitin chains act as the main targeting signals for protein
degradation by the proteasome. Here we report selective binding of AIRAPL, a
protein that associates with the proteasome upon exposure to arsenite, to
Lys48-linked tri-ubiquitin chains. AIRAPL comprises two ubiquitin-interacting
motifs in tandem (tUIMs) that are linked through a flexible inter-UIM region. In
the complex crystal structure UIM1 binds the proximal ubiquitin, whereas UIM2
(the double-sided UIM) binds non-symmetrically to the middle and distal
ubiquitin moieties on either side of the helix. Specificity of AIRAPL
for Lys48-linked ubiquitin chains is determined by UIM2, and the flexible
inter-UIM linker increases avidity by placing the two UIMs in an orientation
that facilitates binding of the third ubiquitin to UIM1. Unlike middle and
proximal ubiquitins, distal ubiquitin binds UIM2 through a novel surface, which
leaves the Ile44 hydrophobic patch accessible for binding to the proteasomal
ubiquitin receptors.
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