3-DIMENSIONAL STRUCTURE OF A HUMAN-IMMUNOGLOBULIN WITH A HINGE DELETION
3-DIMENSIONAL STRUCTURE OF A HUMAN-IMMUNOGLOBULIN WITH A HINGE DELETION
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DOI：
10.1073/pnas.90.9.4271
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发表时间：
1993-05-01
影响因子：
11.1
通讯作者：
EDMUNDSON, AB
中科院分区：
文献类型：
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作者：
GUDDAT, LW;HERRON, JN;EDMUNDSON, AB
3.2埃分辨率的X射线分析表明，MCG-IgG1(波长链)免疫球蛋白是一个致密的T形分子。由于铰链缺失，Fc片段叶被紧紧向上拉入Fab臂的连接处。沿着分子二重轴，FAB臂通过两个轻链之间的链间二硫键连接。抗原结合部位由Fab区顶端的大的不规则空洞组成。Fc上的潜在补体(C1q)结合部位是由Fab臂立体屏蔽的，但可能的结合部位可与人单核细胞上的FcRI受体和金黄色葡萄球菌的A蛋白对接。
X-ray analysis at 3.2-angstrom resolution revealed that the Mcg IgG1 (lambda chain) immunoglobulin is a compact T-shaped molecule. Because of the hinge deletion, the Fc fragment lobe is pulled tightly upward into the junction of the Fab arms. Along the molecular twofold axis, the Fab arms are joined by an interchain disulfide bond between the two light chains. The antigen combining sites consist of large irregular cavities at the tips of the Fab regions. Potential complement (C1q) binding sites on Fc are sterically shielded by the Fab arms, but putative attachment sites are accessible for docking with the FcRI receptor on human monocytes and with protein A of Staphylococcus aureus.