PDBsum entry 2oic

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Transferase PDB id
Protein chains
279 a.a. *
STU ×4
Waters ×269
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of irak4 kinase domain complexed with staurosporine
Structure: Interleukin-1 receptor-associated kinase 4. Chain: a, b, c, d. Fragment: kinase domain. Synonym: irak-4, ny- ren-64 antigen. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: irak4. Expressed in: unidentified baculovirus. Expression_system_taxid: 10469
2.40Å     R-factor:   0.226     R-free:   0.278
Authors: A.Kuglstatter,A.G.Villasenor,M.F.Browner
Key ref: A.Kuglstatter et al. (2007). Cutting Edge: IL-1 receptor-associated kinase 4 structures reveal novel features and multiple conformations. J Immunol, 178, 2641-2645. PubMed id: 17312103
10-Jan-07     Release date:   20-Mar-07    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q9NWZ3  (IRAK4_HUMAN) -  Interleukin-1 receptor-associated kinase 4
460 a.a.
279 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.  - Non-specific serine/threonine protein kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a protein = ADP + a phosphoprotein
+ protein
+ phosphoprotein
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     protein phosphorylation   1 term 
  Biochemical function     transferase activity, transferring phosphorus-containing groups     3 terms  


J Immunol 178:2641-2645 (2007)
PubMed id: 17312103  
Cutting Edge: IL-1 receptor-associated kinase 4 structures reveal novel features and multiple conformations.
A.Kuglstatter, A.G.Villaseñor, D.Shaw, S.W.Lee, S.Tsing, L.Niu, K.W.Song, J.W.Barnett, M.F.Browner.
IL-1R-associated kinase (IRAK)4 plays a central role in innate and adaptive immunity, and is a crucial component in IL-1/TLR signaling. We have determined the crystal structures of the apo and ligand-bound forms of human IRAK4 kinase domain. These structures reveal several features that provide opportunities for the design of selective IRAK4 inhibitors. The N-terminal lobe of the IRAK4 kinase domain is structurally distinctive due to a loop insertion after an extended N-terminal helix. The gatekeeper residue is a tyrosine, a unique feature of the IRAK family. The IRAK4 structures also provide insights into the regulation of its activity. In the apo structure, two conformations coexist, differing in the relative orientation of the two kinase lobes and the position of helix C. In the presence of an ATP analog only one conformation is observed, indicating that this is the active conformation.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20632993 C.C.Lee, Y.Jia, N.Li, X.Sun, K.Ng, E.Ambing, M.Y.Gao, S.Hua, C.Chen, S.Kim, P.Y.Michellys, S.A.Lesley, J.L.Harris, and G.Spraggon (2010).
Crystal structure of the ALK (anaplastic lymphoma kinase) catalytic domain.
  Biochem J, 430, 425-437.
PDB codes: 3l9p 3lcs 3lct
19430930 H.Suhir, and A.Etzioni (2010).
The role of Toll-like receptor signaling in human immunodeficiencies.
  Clin Rev Allergy Immunol, 38, 11-19.  
19752193 U.Maitra, J.S.Parks, and L.Li (2009).
An innate immunity signaling process suppresses macrophage ABCA1 expression through IRAK-1-mediated downregulation of retinoic acid receptor alpha and NFATc2.
  Mol Cell Biol, 29, 5989-5997.  
18691762 D.Wang, S.Fasciano, and L.Li (2008).
The interleukin-1 receptor associated kinase 1 contributes to the regulation of NFAT.
  Mol Immunol, 45, 3902-3908.  
18266302 M.Koziczak-Holbro, A.Glück, C.Tschopp, J.C.Mathison, and H.Gram (2008).
IRAK-4 kinase activity-dependent and -independent regulation of lipopolysaccharide-inducible genes.
  Eur J Immunol, 38, 788-796.  
17979850 S.Y.Zhang, E.Jouanguy, V.Sancho-Shimizu, H.von Bernuth, K.Yang, L.Abel, C.Picard, A.Puel, and J.L.Casanova (2007).
Human Toll-like receptor-dependent induction of interferons in protective immunity to viruses.
  Immunol Rev, 220, 225-236.  
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 codes are shown on the right.