Shape complementarity at protein/protein interfaces.
A new statistic Sc, which has a number of advantages over other measures of packing, is used to examine the shape complementarity of protein/protein interfaces selected from the Brookhaven Protein Data Bank. It is shown using Sc that antibody/antigen interfaces as a whole exhibit poorer shape complementarity than is observed in other systems involving protein/protein interactions. This result can be understood in terms of the fundamentally different evolutionary history of particular antibody/antigen associations compared to other systems considered, and in terms of the differing chemical natures of the interfaces.
Lawrence
M C
MC
Biomolecular Research Institute, Parkville, Victoria, Australia.
Colman
P M
PM
D000937:Antigen-Antibody Reactions; D006454:Hemoglobins / Q000737:chemistry; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry; D046911:Macromolecular Substances; D008958:Models, Molecular; D009439:Neuraminidase / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
D006454:Hemoglobins; D007140:Immunoglobulin Fab Fragments; D046911:Macromolecular Substances; D011506:Proteins; C100003:deoxyhemoglobin; D009439:Neuraminidase