Webster D M, Pedersen J, Staunton D, Jones A, Rees A R
Department of Biochemistry, University of Bath, Claverton Down, UK.
Appl Biochem Biotechnol. 1994 May-Jun;47(2-3):119-32; discussion 132-4. doi: 10.1007/BF02787929.
The antibody repertoire is very large with at least 10(9) different antibody specificities, yet there are currently only 800 variable-region sequences known and < 23 Fab structures deposited with the Brookhaven Protein Data Bank. To engineer the antibody-combining site rationally, we need to define the rules that govern antibody structure. To understand the process of antibody-antigen recognition, we need not only to predict complementary determining regions accurately, but to simulate accurately the interaction of antibody with antigen. We have made progress in the modeling of antibody-combining sites and in the simulation of antibody complex formation. The combination of these approaches will allow us to extend the natural limits of antibody-combining sites in a more rational manner.
抗体库非常庞大，具有至少10⁹种不同的抗体特异性，但目前已知的可变区序列仅有800种，且存入布鲁克海文蛋白质数据库的Fab结构不到23种。为了合理设计抗体结合位点，我们需要确定支配抗体结构的规则。为了理解抗体 - 抗原识别过程，我们不仅需要准确预测互补决定区，还需要精确模拟抗体与抗原的相互作用。我们在抗体结合位点建模和抗体复合物形成模拟方面取得了进展。这些方法的结合将使我们能够以更合理的方式扩展抗体结合位点的天然限制。
