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PDBsum entry 2nq3
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References listed in PDB file
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Key reference
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Title
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The c2 domain of human itchy homolog e3 ubiquitin protein ligase
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Authors
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J.R.Walker,
G.V.Avvakumov,
S.Xue,
C.Butler-Cole,
P.J.Finerty jr.,
J.Weigelt,
M.Sundstrom,
C.H.Arrowsmith,
A.M.Edwards,
A.Bochkarev,
S.Dhe-Paganon.
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Ref.
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To be Published ...
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Secondary reference #1
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Title
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Human itch is a coregulator of the hematopoietic transcription factor nf-E2.
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Authors
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X.Chen,
S.Wen,
M.N.Fukuda,
N.R.Gavva,
D.Hsu,
T.O.Akama,
T.Yang-Feng,
C.K.Shen.
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Ref.
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Genomics, 2001,
73,
238-241.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Atrophin-1, The drpla gene product, Interacts with two families of ww domain-Containing proteins.
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Authors
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J.D.Wood,
J.Yuan,
R.L.Margolis,
V.Colomer,
K.Duan,
J.Kushi,
Z.Kaminsky,
J.J.Kleiderlein,
A.H.Sharp,
C.A.Ross.
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Ref.
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Mol Cell Neurosci, 1998,
11,
149-160.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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Latent membrane protein 2a of epstein-Barr virus binds ww domain e3 protein-Ubiquitin ligases that ubiquitinate b-Cell tyrosine kinases.
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Authors
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G.Winberg,
L.Matskova,
F.Chen,
P.Plant,
D.Rotin,
G.Gish,
R.Ingham,
I.Ernberg,
T.Pawson.
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Ref.
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Mol Cell Biol, 2000,
20,
8526-8535.
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PubMed id
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Secondary reference #4
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Title
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Interaction between two ubiquitin-Protein isopeptide ligases of different classes, Cblc and aip4/itch.
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Authors
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J.R.Courbard,
F.Fiore,
J.Adélaïde,
J.P.Borg,
D.Birnbaum,
V.Ollendorff.
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Ref.
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J Biol Chem, 2002,
277,
45267-45275.
[DOI no: ]
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PubMed id
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Figure 3.
Fig. 3. Analysis of AIP4 mRNA expression. A commercial
Northern blot membrane was used to establish the AIP4 mRNA
expression pattern in human adult tissues. A 1400-bp probe
corresponding to the N-terminal domain (C2 and WW domain) of the
AIP4 protein was used. A major transcript of 6.0 kb was observed
in most tissue except the bone marrow; AIP4 expression is weaker
in spleen and thymus, and a transcript of 4 kb was seen in
testis.
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Figure 5.
Fig. 5. CBLC interacts with the WW domains of AIP4. A,
yeast two-hybrid analysis of CBLC/AIP4 interaction using several
CBLC and AIP4 construct shows that the proline-rich C-terminal
region (50 amino acids long) of CBLC and the WW domains of AIP4
are required for the interaction. Fusion between GAL4 DBD and
CBLC wild type, mutant of the TKB (RK), mutant of the RING
domain (CA), TKB, or C-terminal proline-rich region were tested
for two-hybrid interaction in AH109 yeast in combination with
fusion between AD of GAL4 with AIP4 C2 or with
the four WW domains of AIP4. GAL4 DBD fusion with lamin and GAL4
AD were used as controls. +, positive interaction; , negative
interaction; ND, not determined. B, pull-down experiment using a
GST-WW domains and a lysate of COS-1 cells expressing EGFP-CBLC
confirms that the four AIP4 WW domains bind to CBLC. Controls
show a binding of EGFP-CBLC to a GST-GRB2 and absence of binding
to GST.
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The above figures are
reproduced from the cited reference
with permission from the ASBMB
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