STRUCTURE OF AN ANTIBODY ANTIGEN COMPLEX - CRYSTAL-STRUCTURE OF THE HYHEL-10 FAB-LYSOZYME COMPLEX
STRUCTURE OF AN ANTIBODY ANTIGEN COMPLEX - CRYSTAL-STRUCTURE OF THE HYHEL-10 FAB-LYSOZYME COMPLEX
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DOI：
10.1073/pnas.86.15.5938
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发表时间：
1989-08-01
影响因子：
11.1
通讯作者：
DAVIES, DR
中科院分区：
文献类型：
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作者：
PADLAN, EA;SILVERTON, EW;DAVIES, DR
抗溶菌酶 HyHEL-10 Fab 和鸡蛋清溶菌酶复合物的晶体结构已确定为标称分辨率 3.0 ANG。溶菌酶上的抗原决定簇（表位）是不连续的，由来自线性序列的四个不同区域的残基组成。它由α-螺旋的暴露残基以及周围的氨基酸组成。表位穿过活性位点裂缝并包含位于该裂缝内的色氨酸。抗体的结合位点大部分是平坦的，具有由两个穿过裂缝的酪氨酸组成的突起。 Fab 的所有六个互补决定区都对结合贡献至少一个残基；框架中的一个残基也与溶菌酶接触。抗体上的收缩残基含有不成比例数量的芳香族侧链。抗体与抗原的接触主要涉及氢键和范德华相互作用；存在一种离子对相互作用，但较弱。
The crystal structure of the complex of the anti-lysozyme HyHEL-10 Fab and hen egg white lysozyme has been determined to a nominal resolution of 3.0 .ANG.. The antigenic determinant (epitope) on the lysozyme is discontinuous, consisting of residues from four different regions of the linear sequence. It consists of the exposed residues of an .alpha.-helix together with surrounding amino acids. The epitope crosses the active-site cleft and includes a tryptophan located within this cleft. The combining site of the antibody is mostly flat with a protuberance made up of two tyrosines that penetrate the cleft. All six complementarity-determining regions of the Fab contribute at least one residue to the binding; one residue from the framework is also in contact with the lysozyme. The contracting residues on the antibody contain a disproportionate number of aromatic side chains. The antibody-antigen contact mainly involves hydrogen bonds and van der Waals interactions; there is one ion-pair interaction but it is weak.