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PDBsum entry 2k6d
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Sh3 domain/ubiquitin
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PDB id
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2k6d
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Contents |
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* Residue conservation analysis
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PDB id:
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| Name: |
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Sh3 domain/ubiquitin
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Title:
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Cin85 sh3-c domain in complex with ubiquitin
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Structure:
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Sh3 domain-containing kinase-binding protein 1. Chain: a. Fragment: cin85 sh3-c domain. Synonym: cbl-interacting protein of 85 kda, human src family kinase- binding protein 1, hsb-1, cd2-binding protein 3, cd2bp3. Engineered: yes. Ubiquitin. Chain: b. Fragment: ubiquitin.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: sh3kbp1, cin85. Expressed in: escherichia coli. Gene: rps27a, uba80, ubcep1, uba52, ubcep2, ubb, ubc.
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NMR struc:
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8 models
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Authors:
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J.Forman-Kay,I.Bezsonova
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Key ref:
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I.Bezsonova
et al.
(2008).
Interactions between the three CIN85 SH3 domains and ubiquitin: implications for CIN85 ubiquitination.
Biochemistry,
47,
8937-8949.
PubMed id:
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Date:
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07-Jul-08
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Release date:
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19-Aug-08
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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:
E.C.?
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Biochemistry
47:8937-8949
(2008)
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PubMed id:
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Interactions between the three CIN85 SH3 domains and ubiquitin: implications for CIN85 ubiquitination.
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I.Bezsonova,
M.C.Bruce,
S.Wiesner,
H.Lin,
D.Rotin,
J.D.Forman-Kay.
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ABSTRACT
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CIN85 is an adaptor protein linking the ubiquitin ligase Cbl and
clathrin-binding proteins in clathrin-mediated receptor endocytosis. The SH3
domains of CIN85 bind to a proline-rich region of Cbl. Here we show that all
three SH3 domains of CIN85 bind to ubiquitin. We also present a data-based
structural model of the CIN85 SH3-C domain in complex with ubiquitin. In this
complex, ubiquitin binds to the canonical interaction surface of the SH3 domain
for proline-rich ligands and mimics the PPII helix, and we provide evidence that
ubiquitin competes with these ligands for binding. We demonstrate that
disruption of ubiquitin binding results in constitutive ubiquitination of CIN85
and an increased level of ubiquitination of EGFR in the absence of EGF
stimulation. These results suggest that competition between Cbl and ubiquitin
binding to CIN85 regulates Cbl function and EGFR endocytosis.
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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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J.Adélaïde,
V.Gelsi-Boyer,
J.Rocquain,
N.Carbuccia,
D.J.Birnbaum,
P.Finetti,
F.Bertucci,
M.J.Mozziconacci,
N.Vey,
D.Birnbaum,
and
M.Chaffanet
(2010).
Gain of CBL-interacting protein, a possible alternative to CBL mutations in myeloid malignancies.
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Leukemia,
24,
1539-1541.
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J.M.Winget,
and
T.Mayor
(2010).
The diversity of ubiquitin recognition: hot spots and varied specificity.
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Mol Cell,
38,
627-635.
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N.Pashkova,
L.Gakhar,
S.C.Winistorfer,
L.Yu,
S.Ramaswamy,
and
R.C.Piper
(2010).
WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins.
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Mol Cell,
40,
433-443.
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PDB code:
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S.Havrylov,
M.J.Redowicz,
and
V.L.Buchman
(2010).
Emerging roles of Ruk/CIN85 in vesicle-mediated transport, adhesion, migration and malignancy.
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Traffic,
11,
721-731.
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J.F.Trempe,
C.X.Chen,
K.Grenier,
E.M.Camacho,
G.Kozlov,
P.S.McPherson,
K.Gehring,
and
E.A.Fon
(2009).
SH3 domains from a subset of BAR proteins define a Ubl-binding domain and implicate parkin in synaptic ubiquitination.
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Mol Cell,
36,
1034-1047.
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PDB code:
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J.L.Ortega-Roldan,
M.R.Jensen,
B.Brutscher,
A.I.Azuaga,
M.Blackledge,
and
N.A.van Nuland
(2009).
Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: application to the CD2AP SH3-C:ubiquitin complex.
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Nucleic Acids Res,
37,
e70.
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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.
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Links
