免疫球蛋白M结合补体的结构基础。
The structural basis for binding of complement by immunoglobulin M.
作者信息
Hurst M M, Volanakis J E, Hester R B, Stroud R M, Bennett J C
出版信息
J Exp Med. 1974 Oct 1;140(4):1117-21. doi: 10.1084/jem.140.4.1117.
Abstract
An insight into the structural features of human IgM that are responsible for its capacity to bind the first component of complement (C) has been obtained by examining the ability of IgM subfragments to bind active C1 (C1). The smallest two fragments found to bind C1 were the major CNBr fragment of the Fc portion of IgM and the C(H)4 fragment of the carboxy-terminal domain. The smallest fragment which fixes C1 has a disaggregated mol wt of 6,800, consists of 60 residues, and contains no carbohydrate. Structural considerations and sequence overlaps suggest that the amino-terminal side of the C(H)4 domain (24 amino acid residues) might be responsible for fixing C1.
摘要
通过检测IgM亚片段结合活性C1（C1）的能力，已对人类IgM的结构特征有所洞察，这些结构特征决定了其结合补体（C）第一成分的能力。发现能结合C1的最小两个片段是IgM Fc部分的主要溴化氰片段和羧基末端结构域的C(H)4片段。能固定C1的最小片段解聚分子量为6800，由60个残基组成，且不含碳水化合物。结构方面的考虑和序列重叠表明，C(H)4结构域的氨基末端一侧（24个氨基酸残基）可能负责固定C1。
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