Shape complementarity at protein/protein interfaces

J Mol Biol. 1993 Dec 20;234(4):946-50. doi: 10.1006/jmbi.1993.1648.


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.

MeSH terms

  • Antigen-Antibody Reactions*
  • Hemoglobins / chemistry
  • Immunoglobulin Fab Fragments / chemistry
  • Macromolecular Substances
  • Models, Molecular
  • Neuraminidase / chemistry
  • Protein Binding*
  • Protein Conformation*
  • Proteins / chemistry*


  • Hemoglobins
  • Immunoglobulin Fab Fragments
  • Macromolecular Substances
  • Proteins
  • deoxyhemoglobin
  • Neuraminidase