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Scientists reveal the key mechanisms for affinity between transient binding proteins
Date:7/2/2008

, and establishing rules from them. "One of the conclusions from the study is that what determines that two proteins recognise each other as binding partners falls outside the lineal contact motif, in what is called the context", explains Aloy. The contextual residues are amino acids that are found in nearby regions of the lineal motif but do not form part of it. "The binding strength between two proteins is determined by contacts found in the lineal motif but it is the contextual residues that hold information about the most suitable proteins, thereby preventing undesirable binding between similar proteins", explains Amelie Stein, a pre-doctoral student with Aloy's lab and first author of the article.

The analysis performed by the researchers has also revealed that in certain conditions non native interactions may occur, that is to say, interactions with other proteins that are not optimum. "This is what we refer to as complementary partners, other interaction proteins that can compensate for the lack of the ideal protein", explains Stein. According to the researchers, these non-optimum interactions allow the establishment of emergency circuits that increase the strength of cellular networks. Specifically, one line of research derived from the study by Aloy and Stein focuses on the identification of proteins unable to establish safety circuits and therefore with a good chance of becoming future therapeutic targets.


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Contact: Snia Armengou
sonia.armengou@irbbarcelona.org
34-934-037-255
Institute for Research in Biomedicine (IRB Barcelona)
Source:Eurekalert

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