Authors: R P Bahadur M Zacharias
Publish Date: 2007/12/15
Volume: 65, Issue: 7-8, Pages: 1059-1072
Abstract
Specific proteinprotein interactions are essential for cellular functions Experimentally determined threedimensional structures of proteinprotein complexes offer the possibility to characterize binding interfaces in terms of size shape and packing density Comparison with crystalpacking interfaces representing nonspecific proteinprotein contacts gives insight into how specific binding differs from nonspecific lowaffinity binding An overview is given on empirical structural rules for specific proteinprotein recognition derived from known complex structures Although single parameters such as interface size shape or surface complementary show clear trends for different interface types each parameter alone is insufficient to fully distinguish between specific versus crystalpacking contacts A combination of interface parameters is however well suited to characterize a specific interface This knowledge provides us with the essential ingredients that make up a specific protein recognition site It is also of great value for the prediction of protein binding sites and for the evaluation of predicted complex structures
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