Structural basis of BLyS receptor recognition
Structural basis of BLyS receptor recognition
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DOI：
10.1038/nsb769
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发表时间：
2002-04-01
期刊：
影响因子：
--
通讯作者：
Arnold, E
中科院分区：
文献类型：
--
作者：
Oren, DA;Li, YL;Arnold, E
B淋巴细胞刺激因子（BLyS）是肿瘤坏死因子（TNF）超家族的成员，是一种诱导B细胞增殖和免疫球蛋白分泌的细胞因子。我们以2.0埃的分辨率确定了BLyS的三维结构，并使用有限的蛋白水解结合质谱法鉴定了受体识别片段。与其他结构确定的tnf样配体类似，BLyS单体是一个β -三明治并寡聚形成同型三聚体。与其他细胞因子相比，BLyS中的受体结合区有更深、更明显的凹槽。沟槽底部的保守元素允许细胞因子识别几种结构相关的受体，而沟槽壁和外缘的变化赋予受体特异性。
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 Angstrom 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 beta-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.