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Protein‐protein interactions as a target for drugs in proteomics
Author(s) -
Archakov Alexander I.,
Govorun Vadim M.,
Dubanov Alexander V.,
Ivanov Yuri D.,
Veselovsky Alexander V.,
Lewi Paul,
Janssen Paul
Publication year - 2003
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200390053
Subject(s) - proteomics , protein–protein interaction , protein folding , protein structure , chemistry , biophysics , protein domain , folding (dsp implementation) , computational biology , biology , biochemistry , gene , electrical engineering , engineering
Protein‐protein interactions play a central role in numerous processes in the cell and are one of the main fields of functional proteomics. This review highlights the methods of bioinformatics and functional proteomics of protein‐protein interaction investigation. The structures and properties of contact surfaces, forces involved in protein‐protein interactions, kinetic and thermodynamic parameters of these reactions were considered. The properties of protein contact surfaces depend on their functions. The contact surfaces of permanent complexes resemble domain contacts or the protein core and it is reasonable to consider such complex formation as a continuation of protein folding. Characteristics of contact surfaces of temporary protein complexes share some similarities with active sites of enzymes. The contact surfaces of the temporary protein complexes have unique structure and properties and they are more conservative in comparison with active site of enzymes. So they represent prospective targets for a new generation of drugs. During the last decade, numerous investigations were undertaken to find or design small molecules that block protein dimerization or protein(peptide)‐receptor interaction, or, on the contrary, to induce protein dimerization.