Journal
BIOINFORMATICS
Volume 23, Issue 17, Pages 2203-2209Publisher
OXFORD UNIV PRESS
DOI: 10.1093/bioinformatics/btm323
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Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM058187] Funding Source: NIH RePORTER
- NIGMS NIH HHS [GM058187] Funding Source: Medline
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Motivation: 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. Summary: 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. Contact: zhou@sb.fsu.edu.
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