THE STRUCTURE OF A COMPLEX BETWEEN THE NC10 ANTIBODY AND INFLUENZA-VIRUS NEURAMINIDASE AND COMPARISON WITH THE OVERLAPPING BINDING-SITE OF THE NC41 ANTIBODY
THE STRUCTURE OF A COMPLEX BETWEEN THE NC10 ANTIBODY AND INFLUENZA-VIRUS NEURAMINIDASE AND COMPARISON WITH THE OVERLAPPING BINDING-SITE OF THE NC41 ANTIBODY
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DOI：
10.1016/s0969-2126(00)00074-5
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发表时间：
1994-08-15
期刊：
影响因子：
5.7
通讯作者：
COLMAN, PM
中科院分区：
文献类型：
--
作者：
MALBY, RL;TULIP, WR;COLMAN, PM
背景资料：尽管众所周知，可以针对特定抗原，甚至针对抗原上的特定位点产生不同的抗体，但直到现在还没有对这种类型的交叉反应抗体的结构研究。一种已知结构的抗体-抗原复合物是流感病毒抗原神经氨酸酶与NC 41抗体的复合物，另一种抗神经氨酸酶抗体NC 10，与抗原上的重叠位点结合。本文描述了这种抗体与神经氨酸酶形成的复合物的结构，并与含有NC 41的复合物进行了比较。结果：NC 10 Fab-神经氨酸酶复合物的晶体结构已被细化到2.5埃的标称分辨率。神经氨酸酶上NC 10抗体的约80%的结合位点与NC 41抗体的结合位点重叠。神经氨酸酶的表位残基通常与两种抗体进行完全不同的相互作用。虽然NC 10和NC 41抗体在其重链的第一互补决定区内具有相同的氨基酸序列，但这不是交叉reaction.Conclusions的基础：两种不同蛋白质结合到第三种蛋白质上的相同靶结构的能力不需要基于这些蛋白质内相同或同源氨基酸序列的存在。正如我们已经证明的那样，共同目标结构上的氨基酸残基可能处于完全不同的化学环境中，并且也可能在两种蛋白质-蛋白质复合物中采用不同的构象。
Background: While it is well known that different antibodies can be produced against a particular antigen, and even against a particular site on an antigen up until now there have been no structural studies of cross-reacting antibodies of this type One antibody-antigen complex whose structure is known is that of the influenza virus antigen, neuraminidase, in complex with the NC41 antibody, Another anti-neuraminidase antibody, NC10, binds to an overlapping site on the antigen. The structure of the complex formed by this antibody with neuraminidase is described here and compared with the NC41-containing complex.Results: The crystal structure of the NC10 Fab-neuraminidase complex has been refined to a nominal resolution of 2.5 Angstrom. Approximately 80% of the binding site of the NC10 antibody on neuraminidase overlaps with that of the NC41 antibody. The epitope residues of neuraminidase are often engaged in quite different interactions with the two antibodies. Although the NC10 and NC41 antibodies have identical amino acid sequences within the first complementarity determining region of their heavy chains, this is not the basis of the cross-reaction.Conclusions: The capacity of two different proteins to bind to the same target structure on a third protein need not be based on the existence of identical or homologous amino acid sequences within those proteins. As we have demonstrated, amino acid residues on the common target structure may be in quite different chemical environments, and may also adopt different conformations within two protein-protein complexes.