PDBsum entry 1yiu

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protein links
Ligase PDB id
Protein chain
37 a.a. *
* Residue conservation analysis
PDB id:
Name: Ligase
Title: Itch e3 ubiquitin ligase ww3 domain
Structure: Itchy e3 ubiquitin protein ligase. Chain: a. Fragment: ww3. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: itch e3 ww3 domain. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
NMR struc: 8 models
Authors: A.Z.Shaw,P.Martin-Malpartida,B.Morales,F.Yraola,M.Royo, M.J.Macias
Key ref:
A.Z.Shaw et al. (2005). Phosphorylation of either Ser16 or Thr30 does not disrupt the structure of the Itch E3 ubiquitin ligase third WW domain. Proteins, 60, 558-560. PubMed id: 15971201 DOI: 10.1002/prot.20466
13-Jan-05     Release date:   02-Aug-05    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q8C863  (ITCH_MOUSE) -  E3 ubiquitin-protein ligase Itchy
864 a.a.
37 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 3 residue positions (black crosses)


DOI no: 10.1002/prot.20466 Proteins 60:558-560 (2005)
PubMed id: 15971201  
Phosphorylation of either Ser16 or Thr30 does not disrupt the structure of the Itch E3 ubiquitin ligase third WW domain.
A.Z.Shaw, P.Martin-Malpartida, B.Morales, F.Yraola, M.Royo, M.J.Macias.
No abstract given.

  Selected figure(s)  
Figure 1.
Figure 1. a: Itch-ww3 sequence. Two possible sites identified by NetPhos 2.0 phosphorylation prediction server are indicated in red. The immediate amino acid environment of Thr30 is typical of a phosphorylation site for Casein kinase II, CK2, whereas protein kinase A, PKA is predicted to phosphorylate both Thr30 and Ser16. b: A ribbon representation of Itch-ww3 domain showing the side chains of conserved aromatic residues in magenta. Ser16 and Thr30 are displayed in gold. The stereo-view of the best-fit backbone superposition of 10 NMR derived structures selected according to the lowest energy is shown in the Supplementary Material. The structures are displayed with MOLMOL.[20] c: Selected region of 2D NOESY experiments carried out in D[2]O, showing a characteristic pattern of - NOEs found in the WW fold. 1 corresponds to T30-V23, 2 to K12-F22, 3 to N24-W10, and 4 T14-V20. A table containing the proton chemical shifts of the three domains is given as Supplementary Material.
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 60, 558-560) copyright 2005.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
17437719 B.Morales, X.Ramirez-Espain, A.Z.Shaw, P.Martin-Malpartida, F.Yraola, E.Sánchez-Tilló, C.Farrera, A.Celada, M.Royo, and M.J.Macias (2007).
NMR structural studies of the ItchWW3 domain reveal that phosphorylation at T30 inhibits the interaction with PPxY-containing ligands.
  Structure, 15, 473-483.
PDB codes: 2jo9 2joc
17766370 T.Sharpe, A.L.Jonsson, T.J.Rutherford, V.Daggett, and A.R.Fersht (2007).
The role of the turn in beta-hairpin formation during WW domain folding.
  Protein Sci, 16, 2233-2239.  
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