title: Shape complementarity at protein/protein interfaces.
abstract: 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.
authors.affiliation: Biomolecular Research Institute, Parkville, Victoria, Australia.
authors.forename: M C
authors.initials: MC
authors.lastname: Lawrence
authors.forename: P M
authors.initials: PM
authors.lastname: Colman
mesh_terms: 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*
chemical_list: D006454:Hemoglobins; D007140:Immunoglobulin Fab Fragments; D046911:Macromolecular Substances; D011506:Proteins; C100003:deoxyhemoglobin; D009439:Neuraminidase