Review
Protein–protein interactions: mechanisms and modification by drugs
Article first published online: 6 DEC 2002
DOI: 10.1002/jmr.597
Copyright © 2002 John Wiley & Sons, Ltd.
Additional Information
How to Cite
Veselovsky, A. V., Ivanov, Yu. D., Ivanov, A. S., Archakov, A. I., Lewi, P. and Janssen, P. (2002), Protein–protein interactions: mechanisms and modification by drugs. J. Mol. Recognit., 15: 405–422. doi: 10.1002/jmr.597
Publication History
- Issue published online: 6 DEC 2002
- Article first published online: 6 DEC 2002
- Manuscript Accepted: 28 JUN 2002
- Manuscript Revised: 18 MAR 2002
- Manuscript Received: 8 JAN 2002
Funded by
- RFBR. Grant Numbers: N 99-04-48081, N 01-04-48128
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Keywords:
- protein–protein interaction;
- protein surface;
- inhibitors;
- drug design;
- antagonist;
- protein complex;
- thermodynamics;
- dimerization
Abstract
Protein–protein interactions form the proteinaceous network, which plays a central role in numerous processes in the cell. This review highlights the main structures, properties of contact surfaces, and forces involved in protein–protein interactions. The properties of protein contact surfaces depend on their functions. The characteristics of contact surfaces of short-lived protein complexes share some similarities with the active sites of enzymes. The contact surfaces of permanent complexes resemble domain contacts or the protein core. It is reasonable to consider protein–protein complex formation as a continuation of protein folding. The contact surfaces of the protein complexes have unique structure and properties, so they represent prospective targets for a new generation of drugs. During the last decade, numerous investigations have been undertaken to find or design small molecules that block protein dimerization or protein(peptide)–receptor interaction, or on the other hand, induce protein dimerization. Copyright © 2002 John Wiley & Sons, Ltd.

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