Williams A F
MRC Cellular Immunology Unit, Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE, UK.
Immunol Today. 1987;8(10):298-303. doi: 10.1016/0167-5699(87)90016-8.
The superfamily of molecules with immunoglobulin-like domains has recently been gaining new members-largely on the basis of sequence homology. Here Alan Williams reviews this new work and reveals how the comparison of sequence patterns enables decisions on membership to be made. Accommodation of the new structures demands the provision of new categories, and forces the abandonment of the conserved disulphide bond as the last invariant characteristic of an immunoglobulin-type domain. They may, however, provide more dues to the origins and evolution of the immunoglobulin superfamily.
具有免疫球蛋白样结构域的分子超家族最近不断增添新成员——主要基于序列同源性。在此，艾伦·威廉姆斯对这项新研究进行了综述，并揭示了如何通过比较序列模式来决定成员归属。新结构的纳入需要提供新的类别，同时迫使人们摒弃保守二硫键这一免疫球蛋白型结构域的最后一个不变特征。然而，它们可能为免疫球蛋白超家族的起源和进化提供更多线索。
