Katz B A
Axys Pharmaceutical Corporation, South San Francisco, CA 94080, USA.
Biomol Eng. 1999 Dec 31;16(1-4):57-65. doi: 10.1016/s1050-3862(99)00036-4.
Structural and mechanistic determinants of affinity of streptavidin-binding peptide ligands discovered by phage display are reviewed along with the use of streptavidin as a paradigm for structure-based design. A novel way of producing protein-dimerizing ligands in the streptavidin model system is discussed, in which crystal packing topochemically mediates or even catalyzes dimerization of adjacent bound ligands whose reactive ligating groups are presented toward one another in productive orientations in the crystal lattice. Finally, through crystallography on a set of streptavidin complexes with small molecule and peptide ligands at multiple pHs in two space groups, the mechanism by which ligands enhance intersubunit stabilization of the streptavidin tetramer is probed.
本文综述了通过噬菌体展示发现的链霉亲和素结合肽配体亲和力的结构和机制决定因素，以及将链霉亲和素用作基于结构设计范例的情况。讨论了在链霉亲和素模型系统中产生蛋白质二聚化配体的一种新方法，其中晶体堆积通过拓扑化学介导甚至催化相邻结合配体的二聚化，这些配体的反应性连接基团在晶格中以有效的方向相互呈现。最后，通过在两个空间群中对一组链霉亲和素与小分子和肽配体在多个pH值下的复合物进行晶体学研究，探讨了配体增强链霉亲和素四聚体亚基间稳定性的机制。
