PDBsum entry 2rjk

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protein links
Cytokine PDB id
Protein chain
141 a.a. *
Waters ×64
* Residue conservation analysis
PDB id:
Name: Cytokine
Title: Crystal structure of human tl1a extracellular domain c95s mutant
Structure: Tnf superfamily ligand tl1a. Chain: a. Fragment: human tl1a extracellular domain. Synonym: tumor necrosis factor ligand, superfamily, member 15. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Gene: tnfsf15. Expressed in: escherichia coli.
2.30Å     R-factor:   0.213     R-free:   0.265
Authors: C.Zhan,Q.Yan,Y.Patskovsky,W.Shi,U.A.Ramagopal,R.Toro, J.Bonanno,S.G.Nathenson,S.C.Almo
Key ref: C.Zhan et al. (2009). Biochemical and structural characterization of the human TL1A ectodomain. Biochemistry, 48, 7636-7645. PubMed id: 19522538
15-Oct-07     Release date:   26-Aug-08    
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Protein chain
Pfam   ArchSchema ?
O95150  (TNF15_HUMAN) -  Tumor necrosis factor ligand superfamily member 15
251 a.a.
141 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   2 terms 
  Biological process     immune response   3 terms 
  Biochemical function     tumor necrosis factor receptor binding     1 term  


Biochemistry 48:7636-7645 (2009)
PubMed id: 19522538  
Biochemical and structural characterization of the human TL1A ectodomain.
C.Zhan, Q.Yan, Y.Patskovsky, Z.Li, R.Toro, A.Meyer, H.Cheng, M.Brenowitz, S.G.Nathenson, S.C.Almo.
TNF-like 1A (TL1A) is a newly described member of the TNF superfamily that is directly implicated in the pathogenesis of autoimmune diseases, including inflammatory bowel disease, atherosclerosis, and rheumatoid arthritis. We report the crystal structure of the human TL1A extracellular domain at a resolution of 2.5 A, which reveals a jelly-roll fold typical of the TNF superfamily. This structural information, in combination with complementary mutagenesis and biochemical characterization, provides insights into the binding interface and the specificity of the interactions between TL1A and the DcR3 and DR3 receptors. These studies suggest that the mode of interaction between TL1A and DcR3 differs from other characterized TNF ligand/receptor complexes. In addition, we have generated functional TL1A mutants with altered disulfide bonding capability that exhibit enhanced solution properties, which will facilitate the production of materials for future cell-based and whole animal studies. In summary, these studies provide insights into the structure and function of TL1A and provide the basis for the rational manipulation of its interactions with cognate receptors.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20858499 J.Leitner, W.Kuschei, K.Grabmeier-Pfistershammer, R.Woitek, E.Kriehuber, O.Majdic, G.Zlabinger, W.F.Pickl, and P.Steinberger (2010).
T cell stimulator cells, an efficient and versatile cellular system to assess the role of costimulatory ligands in the activation of human T cells.
  J Immunol Methods, 362, 131-141.  
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