PDBsum entry 2o0o

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Cytokine, hormone/growth factor PDB id
Protein chain
153 a.a. *
Waters ×37
* Residue conservation analysis
PDB id:
Name: Cytokine, hormone/growth factor
Title: Crystal structure of tl1a
Structure: Tnf superfamily ligand tl1a. Chain: a, b, c. Synonym: tumor necrosis factor ligand superfamily member 15 engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: tnfsf15. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
3.00Å     R-factor:   0.243     R-free:   0.295
Authors: T.C.Jin,S.Kim,F.Guo,A.J.Howard,Y.Z.Zhang
Key ref: T.Jin et al. (2007). X-ray crystal structure of TNF ligand family member TL1A at 2.1A. Biochem Biophys Res Commun, 364, 1-6. PubMed id: 17935696 DOI: 10.1016/j.bbrc.2007.09.097
27-Nov-06     Release date:   30-Oct-07    
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Protein chains
Pfam   ArchSchema ?
O95150  (TNF15_HUMAN) -  Tumor necrosis factor ligand superfamily member 15
251 a.a.
153 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  


DOI no: 10.1016/j.bbrc.2007.09.097 Biochem Biophys Res Commun 364:1-6 (2007)
PubMed id: 17935696  
X-ray crystal structure of TNF ligand family member TL1A at 2.1A.
T.Jin, F.Guo, S.Kim, A.Howard, Y.Z.Zhang.
The TNF family has been one of the most intensively studied protein families in the past two decades and it has rapidly expanded through the era of genomics and bioinformatics. However, the structural basis of the functional and interactional similarities and differences of this family is poorly understood. TL1A is a recently identified TNF family member that has received increasing attention. Here, the crystal structure of human TL1A is reported. TL1A forms a homotrimer with each monomer assuming a jellyroll beta-sandwich fold. The CD loop in TL1A is the longest among the TNF ligand members with known structure and the AA' loop in TL1A is the second longest after that in TRAIL, where part of it is disordered. Both these loops are known to participate in receptor binding in TNFbeta/LTalpha. The AA' loop may be very different in other TL1A variants if the overall fold is to be preserved.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20675618 C.Mück, D.Herndler-Brandstetter, L.Micutkova, B.Grubeck-Loebenstein, and P.Jansen-Dürr (2010).
Two functionally distinct isoforms of TL1A (TNFSF15) generated by differential ectodomain shedding.
  J Gerontol A Biol Sci Med Sci, 65, 1165-1180.  
  20052682 X.Chen, J.Wu, H.Liu, Z.He, M.Gu, N.Wang, J.Ma, J.Hu, L.Xia, H.He, J.Yuan, J.Li, L.Li, M.Li, and X.Zhu (2010).
Approaches to efficient production of recombinant angiogenesis inhibitor rhVEGI-192 and characterization of its structure and antiangiogenic function.
  Protein Sci, 19, 449-457.  
19522538 C.Zhan, Q.Yan, Y.Patskovsky, Z.Li, R.Toro, A.Meyer, H.Cheng, M.Brenowitz, S.G.Nathenson, and S.C.Almo (2009).
Biochemical and structural characterization of the human TL1A ectodomain.
  Biochemistry, 48, 7636-7645.
PDB codes: 2qe3 2rjk 2rjl
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