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PDBsum entry 5hqg
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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 basis for substrate selectivity of the e3 ligase cop1.
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Authors
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S.Uljon,
X.Xu,
I.Durzynska,
S.Stein,
G.Adelmant,
J.A.Marto,
W.S.Pear,
S.C.Blacklow.
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Ref.
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Structure, 2016,
24,
687-696.
[DOI no: ]
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PubMed id
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Abstract
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COP1 proteins are E3 ubiquitin ligases that regulate phototropism in plants and
target transcription factors for degradation in mammals. The substrate-binding
region of COP1 resides within a WD40-repeat domain that also binds to Trib
proteins, which are adaptors for C/EBPα degradation. Here we report structures
of the human COP1 WD40 domain in isolation, and complexes of the human and
Arabidopsis thaliana COP1 WD40 domains with the binding motif of Trib1. The
human and Arabidopsis WD40 domains are seven-bladed β propellers with an
inserted loop on the bottom face of the first blade. The Trib1 peptide binds in
an extended conformation to a highly conserved surface on the top face of the β
propeller, indicating a general mode for recognition of peptide motifs by COP1.
Together, these studies identify the structural basis and key interactions
for motif recognition by COP1, and hint at how Trib1 autoinhibition is overcome
to target C/EBPα for degradation.
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