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• W2152848278 abstract "Abstract Finding why protein–protein interactions (PPIs) are so specific can provide a valuable tool in a variety of fields. Statistical surveys of so‐called transient complexes (like those relevant for signal transduction mechanisms) have shown a tendency of polar residues to participate in the interaction region. Following this scheme, residues in the unbound partners have to compete between interacting with water or interacting with other residues of the protein. On the other hand, several works have shown that the notion of active site electrostatic preorganization can be used to interpret the high efficiency in enzyme reactions. This preorganization can be related to the instability of the residues important for catalysis. In some enzymes, in addition, conformational changes upon binding to other proteins lead to an increase in the activity of the enzymatic partner. In this article the linear response approximation version of the semimacroscopic protein dipoles Langevin dipoles (PDLD/S‐LRA) model is used to evaluate the stability of several residues in two phosphate hydrolysis enzymes upon complexation with their activating partners. In particular, the residues relevant for PPI and for phosphate hydrolysis in the CDK2/Cyclin A and Ras/GAP complexes are analyzed. We find that the evaluation of the stability of residues in these systems can be used to identify not only active site regions but it can also be used as a guide to locate “hot spots” for PPIs. We also show that conformational changes play a major role in positioning interfacing residues in a proper “energetic” orientation, ready to interact with the residues in the partner protein surface. Thus, we extend the preorganization theory to PPIs, extrapolating the results we obtained from the above‐mentioned complexes to a more general case. We conclude that the correlation between stability of a residue in the surface and the likelihood that it participates in the interaction can be a general fact for transient PPIs. Proteins 2006. © 2005 Wiley‐Liss, Inc." @default.
• W2152848278 created "2016-06-24" @default.
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• W2152848278 date "2005-12-22" @default.
• W2152848278 modified "2023-10-10" @default.
• W2152848278 title "The role of residue stability in transient protein-protein interactions involved in enzymatic phosphate hydrolysis. A computational study" @default.
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• W2152848278 doi "https://doi.org/10.1002/prot.20791" @default.
• W2152848278 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16374872" @default.
• W2152848278 hasPublicationYear "2005" @default.
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