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PDBsum entry 2nq3

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Ligase PDB id
2nq3
Contents
Protein chain
131 a.a.
Metals
_CL
Waters ×128

References listed in PDB file
Key reference
Title The c2 domain of human itchy homolog e3 ubiquitin protein ligase
Authors 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.
Ref. To be Published ...
Secondary reference #1
Title Human itch is a coregulator of the hematopoietic transcription factor nf-E2.
Authors X.Chen, S.Wen, M.N.Fukuda, N.R.Gavva, D.Hsu, T.O.Akama, T.Yang-Feng, C.K.Shen.
Ref. Genomics, 2001, 73, 238-241. [DOI no: 10.1006/geno.2001.6512]
PubMed id 11318614
Full text Abstract
Secondary reference #2
Title Atrophin-1, The drpla gene product, Interacts with two families of ww domain-Containing proteins.
Authors 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.
Ref. Mol Cell Neurosci, 1998, 11, 149-160. [DOI no: 10.1006/mcne.1998.0677]
PubMed id 9647693
Full text Abstract
Secondary reference #3
Title Latent membrane protein 2a of epstein-Barr virus binds ww domain e3 protein-Ubiquitin ligases that ubiquitinate b-Cell tyrosine kinases.
Authors G.Winberg, L.Matskova, F.Chen, P.Plant, D.Rotin, G.Gish, R.Ingham, I.Ernberg, T.Pawson.
Ref. Mol Cell Biol, 2000, 20, 8526-8535.
PubMed id 11046148
Abstract
Secondary reference #4
Title Interaction between two ubiquitin-Protein isopeptide ligases of different classes, Cblc and aip4/itch.
Authors J.R.Courbard, F.Fiore, J.Adélaïde, J.P.Borg, D.Birnbaum, V.Ollendorff.
Ref. J Biol Chem, 2002, 277, 45267-45275. [DOI no: 10.1074/jbc.M206460200]
PubMed id 12226085
Full text Abstract
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.
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.
The above figures are reproduced from the cited reference with permission from the ASBMB
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