Nature Structural Biology9, 288 - 292 (2002)
Published online: 25 February 2002; | doi:10.1038/nsb769
Structural basis of BLyS receptor recognition
Deena A. Oren1, Yuling Li2, Yulia Volovik1, Tina S. Morris2, Chhaya Dharia1, Kalyan Das1, Olga Galperina2, Reiner Gentz2
& Eddy Arnold1
1
Center for Advanced Biotechnology and Medicine and Department of Chemistry and Chemical Biology, Rutgers University, 679 Hoes Lane, Piscataway, New Jersey 08816, USA.
2
Department of Protein Development, Human Genome Sciences, 9410 Key West Avenue, Rockville, Maryland 20850, USA.
B lymphocyte stimulator (BLyS), a member of the tumor necrosis factor (TNF) superfamily, is a cytokine that induces B-cell proliferation and immunoglobulin secretion. We have determined the three-dimensional structure of BLyS to 2.0 Å resolution and identified receptor recognition segments using limited proteolysis coupled with mass spectrometry. Similar to other structurally determined TNF-like ligands, the BLyS monomer is a -sandwich and oligomerizes to form a homotrimer. The receptor-binding region in BLyS is a deeper, more pronounced groove than in other cytokines. The conserved elements on the 'floor' of this groove allow for cytokine recognition of several structurally related receptors, whereas variations on the 'walls' and outer rims of the groove confer receptor specificity.
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-sandwich and oligomerizes to form a homotrimer. The receptor-binding region in BLyS is a deeper, more pronounced groove than in other cytokines. The conserved elements on the 'floor' of this groove allow for cytokine recognition of several structurally related receptors, whereas variations on the 'walls' and outer rims of the groove confer receptor specificity.
