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* Residue conservation analysis
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PDB id:
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Ligase
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Title:
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Insights into scf ubiquitin ligases from the structure of the skp1- skp2 complex
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Structure:
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Cyclin a/cdk2-associated p19. Chain: a, c. Fragment: residues 101-153. Synonym: skp2 f-box. Engineered: yes. Cyclin a/cdk2-associated p45. Chain: b, d. Fragment: residues 1-147. Synonym: skp1.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
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Biol. unit:
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Tetramer (from
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Resolution:
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1.80Å
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R-factor:
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0.218
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R-free:
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0.274
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Authors:
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B.A.Schulman,A.C.Carrano,P.D.Jeffrey,Z.Bowen,E.R.E.Kinnucan, M.S.Finnin,S.J.Elledge,J.W.Harper,M.Pagano,N.P.Pavletich
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Key ref:
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B.A.Schulman
et al.
(2000).
Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex.
Nature,
408,
381-386.
PubMed id:
DOI:
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Date:
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08-Sep-00
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Release date:
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29-Nov-00
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, B, C, D:
E.C.?
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DOI no:
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Nature
408:381-386
(2000)
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PubMed id:
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Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex.
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B.A.Schulman,
A.C.Carrano,
P.D.Jeffrey,
Z.Bowen,
E.R.Kinnucan,
M.S.Finnin,
S.J.Elledge,
J.W.Harper,
M.Pagano,
N.P.Pavletich.
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ABSTRACT
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F-box proteins are members of a large family that regulates the cell cycle, the
immune response, signalling cascades and developmental programmes by targeting
proteins, such as cyclins, cyclin-dependent kinase inhibitors, IkappaBalpha and
beta-catenin, for ubiquitination (reviewed in refs 1-3). F-box proteins are the
substrate-recognition components of SCF (Skp1-Cullin-F-box protein)
ubiquitin-protein ligases. They bind the SCF constant catalytic core by means of
the F-box motif interacting with Skp1, and they bind substrates through their
variable protein-protein interaction domains. The large number of F-box proteins
is thought to allow ubiquitination of numerous, diverse substrates. Most
organisms have several Skp1 family members, but the function of these Skp1
homologues and the rules of recognition between different F-box and Skp1
proteins remain unknown. Here we describe the crystal structure of the human
F-box protein Skp2 bound to Skp1. Skp1 recruits the F-box protein through a
bipartite interface involving both the F-box and the substrate-recognition
domain. The structure raises the possibility that different Skp1 family members
evolved to function with different subsets of F-box proteins, and suggests that
the F-box protein may not only recruit substrate, but may also position it
optimally for the ubiquitination reaction.
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Selected figure(s)
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Figure 1.
Figure 1: Structure of the Skp1-Skp2 complex. Skp1 is shown
in blue and Skp2 is shown in red. The boundaries of the BTB/POZ
fold, the C-terminal helical extension of Skp1 and of the F-box,
the three non-canonical LRRs, the seven canonical LRRs and the
C-terminal tail of Skp2 are shown in the diagram below the
structure. The 100-residue N-terminal Skp2 region missing from
the crystallized protein is indicated (dashed line). The second
LRR has a partially disordered loop instead of the helix
characteristic of LRRs.
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Figure 4.
Figure 4: Comparison of the Skp2-Skp1 and VHL-ElonginC-ElonginB
complexes. a, Homologous portions of Skp1 and ElonginC are
aligned and boxed. Skp2 and VHL are red, Skp1 and ElonginC are
blue and ElonginB is green. The LRRs of Skp2 (refs 4, 8, 26, 27)
and the  -domain
of VHL are thought to bind substrate^23. Owing to its unique C
terminus, Skp1 binds the F-box differently from the way that
ElonginC binds VHL. The arrangement of helices in the two
interfaces is similar, although the helices come from
non-corresponding members of the complexes (H1 and H2 from VHL
superimpose with H6 and H7 from Skp1, not helices from Skp2). b,
The ElonginC-binding region of VHL resembles the three-helix
cluster structure of the F-box.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2000,
408,
381-386)
copyright 2000.
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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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A.E.Rose,
G.Wang,
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M.Mazumdar,
E.Hernando,
and
I.Osman
(2011).
Clinical relevance of SKP2 alterations in metastatic melanoma.
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Pigment Cell Melanoma Res,
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A.Sarikas,
T.Hartmann,
and
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(2011).
The cullin protein family.
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Genome Biol,
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ARABIDILLO proteins have a novel and conserved domain structure important for the regulation of their stability.
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Structural regulation of cullin-RING ubiquitin ligase complexes.
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Structure,
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PDB code:
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H.Tada,
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PDB codes:
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PDB code:
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S.Tokarz,
C.Berset,
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PDB codes:
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W.R.Moyle,
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PDB code:
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Mol Cell,
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PDB code:
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K.F.Ahmad,
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Mechanism of SMRT corepressor recruitment by the BCL6 BTB domain.
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Mol Cell,
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PDB codes:
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Nature,
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BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3.
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Cell,
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Mol Biol Cell,
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Mol Cell,
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Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase.
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Cell,
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PDB code:
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W.Krek
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BTB proteins as henchmen of Cul3-based ubiquitin ligases.
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Nat Cell Biol,
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Interaction of Epstein-Barr virus latent membrane protein 1 with SCFHOS/beta-TrCP E3 ubiquitin ligase regulates extent of NF-kappaB activation.
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A negatively charged amino acid in Skp2 is required for Skp2-Cks1 interaction and ubiquitination of p27Kip1.
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COI1 links jasmonate signalling and fertility to the SCF ubiquitin-ligase complex in Arabidopsis.
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Transferable domain in the G(1) cyclin Cln2 sufficient to switch degradation of Sic1 from the E3 ubiquitin ligase SCF(Cdc4) to SCF(Grr1).
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Sgt1p contributes to cyclic AMP pathway activity and physically interacts with the adenylyl cyclase Cyr1p/Cdc35p in budding yeast.
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Three different binding sites of Cks1 are required for p27-ubiquitin ligation.
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J Biol Chem,
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G.Polekhina,
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Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-alpha signaling.
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Nat Struct Biol,
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PDB code:
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K.P.Bencsath,
M.S.Podgorski,
V.R.Pagala,
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Identification of a multifunctional binding site on Ubc9p required for Smt3p conjugation.
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J Biol Chem,
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Mol Cell,
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A ubiquitin-proteasome pathway represses the Drosophila immune deficiency signaling cascade.
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Curr Biol,
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The Caenorhabditis elegans Skp1-related gene family: diverse functions in cell proliferation, morphogenesis, and meiosis.
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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
code is
shown on the right.
|
 |
Links
