title: Interaction-site prediction for protein complexes: a critical assessment.
abstract: BACKGROUND
  Proteins function through interactions with other proteins and biomolecules. Protein-protein interfaces hold key information toward molecular understanding of protein function. In the past few years, there have been intensive efforts in developing methods for predicting protein interface residues. A review that presents the current status of interface prediction and an overview of its applications and project future developments is in order.
  
  
  CONCLUSIONS
  Interface prediction methods rely on a wide range of sequence, structural and physical attributes that distinguish interface residues from non-interface surface residues. The input data are manipulated into either a numerical value or a probability representing the potential for a residue to be inside a protein interface. Predictions are now satisfactory for complex-forming proteins that are well represented in the Protein Data Bank, but less so for under-represented ones. Future developments will be directed at tackling problems such as building structural models for multi-component structural complexes.
authors.affiliation: Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306, USA. zhou@sb.fsu.edu
authors.forename: Huan-Xiang
authors.initials: HX
authors.lastname: Zhou
authors.forename: Sanbo
authors.initials: S
authors.lastname: Qin
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D001665:Binding Sites; D003198:Computer Simulation; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D011506:Proteins / Q000737:chemistry* / Q000648:ultrastructure; D020539:Sequence Analysis, Protein / Q000379:methods*
chemical_list: D011506:Proteins