26-10 FAB-DIGOXIN COMPLEX - AFFINITY AND SPECIFICITY DUE TO SURFACE COMPLEMENTARITY
26-10 FAB-DIGOXIN COMPLEX - AFFINITY AND SPECIFICITY DUE TO SURFACE COMPLEMENTARITY
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DOI：
10.1073/pnas.90.21.10310
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发表时间：
1993-11-01
影响因子：
11.1
通讯作者：
SHERIFF, S
中科院分区：
文献类型：
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作者：
JEFFREY, PD;STRONG, RK;SHERIFF, S
我们已经确定了抗地高辛单克隆抗体26-10的抗原结合片段的三维结构，其在未复合状态下的分辨率为2.7埃，在与地高辛的复合物中的分辨率为2.5埃。抗体和地高辛在形成复合物时均不发生任何显著的构象变化。地高辛主要与抗体重链相互作用，并定向为使碳水化合物基团暴露于溶剂，而内酯环则埋入结合位点底部的深口袋中。尽管抗体和抗原之间存在广泛的相互作用，但在26-10和地高辛之间没有形成氢键或盐键。因此，26-10-地高辛复合物在已知的抗体-抗原复合物的三维结构中是独特的，因为特异性和高亲和力主要来自形状互补性。
We have determined the three-dimensional structures of the antigen-binding fragment of the anti-digoxin monoclonal antibody 26-10 in the uncomplexed state at 2.7 angstrom resolution and as a complex with digoxin at 2.5 angstrom resolution. Neither the antibody nor digoxin undergoes any significant conformational changes upon forming the complex. Digoxin interacts primarily with the antibody heavy chain and is oriented such that the carbohydrate groups are exposed to solvent and the lactone ring is buried in a deep pocket at the bottom of the combining site. Despite extensive interactions between antibody and antigen, no hydrogen bonds or salt links are formed between 26-10 and digoxin. Thus the 26-10-digoxin complex is unique among the known three-dimensional structures of antibody-antigen complexes in that specificity and high affinity arise primarily from shape complementarity.