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Contents |
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402 a.a.
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131 a.a.
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11 a.a.
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* Residue conservation analysis
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PDB id:
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| Name: |
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Signaling protein
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Title:
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Structure of a beta-trcp1-skp1-beta-catenin complex: destruction motif binding and lysine specificity on the scfbeta-trcp1 ubiquitin ligase
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Structure:
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F-box/wd-repeat protein 1a. Chain: a. Synonym: f-box and wd-repeats protein beta-trcp, e3rsikappab, pikappabalpha-e3 receptor subunit. Engineered: yes. Skp1. Chain: b. Engineered: yes. Beta-catenin.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf9. Gene: ctnnb1 or ctnnb.
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Biol. unit:
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Trimer (from
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Resolution:
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2.95Å
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R-factor:
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0.233
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R-free:
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0.286
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Authors:
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G.Wu,G.Xu,B.A.Schulman,P.D.Jeffrey,J.W.Harper,N.P.Pavletich
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Key ref:
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G.Wu
et al.
(2003).
Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase.
Mol Cell,
11,
1445-1456.
PubMed id:
DOI:
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Date:
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14-Apr-03
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Release date:
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08-Jul-03
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PROCHECK
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Headers
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References
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Q9Y297
(FBW1A_HUMAN) -
F-box/WD repeat-containing protein 1A from Homo sapiens
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Seq:
Struc:
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605 a.a.
402 a.a.*
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DOI no:
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Mol Cell
11:1445-1456
(2003)
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PubMed id:
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Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase.
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G.Wu,
G.Xu,
B.A.Schulman,
P.D.Jeffrey,
J.W.Harper,
N.P.Pavletich.
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ABSTRACT
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The SCF ubiquitin ligases catalyze protein ubiquitination in diverse cellular
processes. SCFs bind substrates through the interchangeable F box protein
subunit, with the >70 human F box proteins allowing the recognition of a wide
range of substrates. The F box protein beta-TrCP1 recognizes the doubly
phosphorylated DpSGphiXpS destruction motif, present in beta-catenin and
IkappaB, and directs the SCF(beta-TrCP1) to ubiquitinate these proteins at
specific lysines. The 3.0 A structure of a beta-TrCP1-Skp1-beta-catenin complex
reveals the basis of substrate recognition by the beta-TrCP1 WD40 domain. The
structure, together with the previous SCF(Skp2) structure, leads to the model of
SCF catalyzing ubiquitination by increasing the effective concentration of the
substrate lysine at the E2 active site. The model's prediction that the
lysine-destruction motif spacing is a determinant of ubiquitination efficiency
is confirmed by measuring ubiquitination rates of mutant beta-catenin peptides,
solidifying the model and also providing a mechanistic basis for lysine
selection.
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Selected figure(s)
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Figure 3.
Figure 3. The #-TrCP1-Skp1 Interface Is Similar to that in the Skp1-Skp2 Complex
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Figure 5.
Figure 5. The Rate of Ubiquitination by the SCF
#-TrCP1
Is Dependent on the Spacing between the Ubiquitination-Site Lysine and the Destruction
Motif
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2003,
11,
1445-1456)
copyright 2003.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
|
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|
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A.Werner,
A.Disanza,
N.Reifenberger,
G.Habeck,
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B.Schulman,
G.Scita,
and
F.Melchior
(2012).
SCF(Fbxw5) mediates transient degradation of actin remodeller Eps8 to allow proper mitotic progression.
|
| |
Nat Cell Biol,
15,
179-188.
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B.Kuhlman,
and
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Essential role for ubiquitin-ubiquitin-conjugating enzyme interaction in ubiquitin discharge from Cdc34 to substrate.
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| |
Mol Cell,
42,
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|
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and
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ARABIDILLO proteins have a novel and conserved domain structure important for the regulation of their stability.
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|
C.Xu,
and
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Structure and function of WD40 domain proteins.
|
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Protein Cell,
2,
202-214.
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PDB codes:
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D.M.Duda,
D.C.Scott,
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and
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Structural regulation of cullin-RING ubiquitin ligase complexes.
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and
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Crystal structure of inhibitor of κB kinase β.
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| |
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PDB codes:
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Q.Zhou,
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The ubiquitin-specific protease USP47 is a novel beta-TRCP interactor regulating cell survival.
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WD40 proteins propel cellular networks.
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The Prp19 WD40 domain contains a conserved protein interaction region essential for its function.
|
| |
Structure,
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PDB code:
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|
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C.Xu,
C.Bian,
W.Yang,
M.Galka,
H.Ouyang,
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PDB codes:
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|
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D.C.Scott,
J.K.Monda,
C.R.Grace,
D.M.Duda,
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and
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A dual E3 mechanism for Rub1 ligation to Cdc53.
|
| |
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PDB codes:
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|
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D.Wu,
and
W.Pan
(2010).
GSK3: a multifaceted kinase in Wnt signaling.
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13,
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H.Inuzuka,
A.Tseng,
D.Gao,
B.Zhai,
Q.Zhang,
S.Shaik,
L.Wan,
X.L.Ang,
C.Mock,
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J.M.Stommel,
S.Gygi,
G.Lahav,
J.Asara,
Z.X.Xiao,
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and
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(2010).
Phosphorylation by casein kinase I promotes the turnover of the Mdm2 oncoprotein via the SCF(beta-TRCP) ubiquitin ligase.
|
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|
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|
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|
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J.Liu,
and
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(2010).
Molecular dynamics reveal the essential role of linker motions in the function of cullin-RING E3 ligases.
|
| |
J Mol Biol,
396,
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|
|
|
K.Wu,
J.Kovacev,
and
Z.Q.Pan
(2010).
Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate.
|
| |
Mol Cell,
37,
784-796.
|
|
|
|
|
|
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M.Sadowski,
and
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(2010).
Mechanisms of mono- and poly-ubiquitination: Ubiquitination specificity depends on compatibility between the E2 catalytic core and amino acid residues proximal to the lysine.
|
| |
Cell Div,
5,
19.
|
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R.Suryadinata,
X.Lai,
J.Heierhorst,
and
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(2010).
Molecular basis for lysine specificity in the yeast ubiquitin-conjugating enzyme Cdc34.
|
| |
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30,
2316-2329.
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F.Bajanca,
A.J.Rodrigues,
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and
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and
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Ubiquitination and degradation of the inhibitors of NF-kappaB.
|
| |
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|
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(2010).
Ubiquitylation of the amino terminus of Myc by SCF(β-TrCP) antagonizes SCF(Fbw7)-mediated turnover.
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| |
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12,
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and
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Modulation of SCF beta-TrCP-dependent I kappaB alpha ubiquitination by hydrogen peroxide.
|
| |
J Biol Chem,
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A promiscuous alpha-helical motif anchors viral hijackers and substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery.
|
| |
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PDB codes:
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X.H.Wu,
H.Zhang,
and
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T.Oda,
and
M.Kitagawa
(2009).
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|
| |
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|
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|
X.Li,
J.Liu,
and
T.Gao
(2009).
beta-TrCP-mediated ubiquitination and degradation of PHLPP1 are negatively regulated by Akt.
|
| |
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|
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|
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(2009).
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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