Crystallization and preliminary X-ray crystallographic study of the extracellular domain of the 4-1BB ligand, a member of the TNF family.
The 4-1BB ligand, a member of the tumour necrosis factor (TNF) family, is an important co-stimulatory molecule that plays a key role in the clonal expansion and survival of CD8+ T cells. Signalling through binding of the 4-1BB ligand and 4-1BB has been reported to enhance CD8+ T-cell expansion and protect activated CD8+ T cells from death. The 4-1BB ligand is an integral protein expressed on activated antigen-presenting cells. The extracellular domain of the 4-1BB ligand fused with glutathione-S-transferase was expressed in Escherichia coli (Origami) and purified by using affinity and ion-exchange column chromatographic methods. Crystals of the 4-1BB ligand were obtained at 290 K by the hanging-drop vapour-diffusion method. X-ray diffraction data were collected from these crystals to 2.8 A resolution and the crystals belong to space group C2, with unit-cell parameters a = 114.6, b = 73.8, c = 118.50 A, beta = 115.5 degrees.
Byun
Jung-Sue
JS
Department of Biology, Yonsei University, Seoul 120-749, South Korea.
Kim
Dong-Uk
DU
Ahn
Byungchan
B
Kwon
Byoung Se
BS
Cho
Hyun-Soo
HS
D053330:4-1BB Ligand; D003460:Crystallization; D018360:Crystallography, X-Ray; D005110:Extracellular Space / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D005810:Multigene Family; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry; D048069:Tumor Necrosis Factors / Q000737:chemistry* / Q000235:genetics
D053330:4-1BB Ligand; D011993:Recombinant Fusion Proteins; C505974:TNFSF9 protein, human; D048069:Tumor Necrosis Factors